Some Amino Acid Sequences for IDH

LOCUS 2497259 433 aa 01-NOV-1997

DEFINITION ISOCITRATE DEHYDROGENASE (NADP), CHLOROPLAST PRECURSOR (OXALOSUCCINATE DECARBOXYLASE) (IDH) (NADP+-SPECIFIC ICDH) (IDP).

ACCESSION 2497259

PID g2497259

DB SOURCE SWISS-PROT: locus IDHP_MEDSA, accession Q40345

class: standard.

created: Nov 1, 1997.

sequence updated: Nov 1, 1997.

annotation updated: Nov 1, 1997.

xrefs: gi: 166385, gi: 166386

xrefs (non-sequence databases): PROSITE PS00470

KEYWORDS OXIDOREDUCTASE; NADP; GLYOXYLATE BYPASS; TRICARBOXYLIC ACID CYCLE; TRANSIT PEPTIDE; CHLOROPLAST.

SOURCE Medicago sativa.

ORGANISM Medicago sativa

Eukaryotae; Viridiplantae; Charophyta/Embryophyta group;

Embryophyta; Tracheophyta; seed plants; Magnoliophyta;

eudicotyledons; Rosidae; Fabales; Fabaceae; Papilionoideae;

Medicago.

REFERENCE 1 (residues 1 to 433)

AUTHORS Shorrosh,B.S. and Dixon,R.A.

TITLE Molecular characterization and expression of an isocitrate dehydrogenase from alfalfa (Medicago sativa L)

JOURNAL Plant Mol. Biol. 20 (5), 801-807 (1992)

MEDLINE 93099232

REMARK SEQUENCE FROM N.A.

COMMENT [CATALYTIC ACTIVITY] ISOCITRATE + NADP(+) = 2-OXOGLUTARATE + CO(2)

+ NADPH.

[COFACTOR] REQUIRES MANGANESE OR MAGNESIUM (BY SIMILARITY).

[SUBCELLULAR LOCATION] CHLOROPLAST (POTENTIAL).

[TISSUE SPECIFICITY] DETECTED IN ALL TISSUES EXAMINED.

[SIMILARITY] BELONGS TO THE ISOCITRATE AND ISOPROPYLMALATE

DEHYDROGENASES FAMILY.

FEATURES Location/Qualifiers

source 1..433

/organism="Medicago sativa"

/db_xref="taxon:3879"

Protein <1..433

/product="ISOCITRATE DEHYDROGENASE"

/EC_number="1.1.1.42"

Region <1..21

/note="CHLOROPLAST."

/region_name="Transit peptide"

Region 22..433

/note="ISOCITRATE DEHYDROGENASE (NADP)."

/region_name="Mature chain"

Site 117

/note="BINDING TO ISOCITRATE."

/site_type="active"

ORIGIN

1 qfspnlsfsa ffpiitftta tmgfqkikva npivemdgde mtriiwkyik dklifpfvel

61 dikyfdlglp yrdetndkvt vesaeatlky nvaikcatit pdearvkefg lksmwrspng

121 tirnilngtv frepiickni prlipgwtkp icigrhafgd qyratdsvik gpgklklvfv

181 pegqgettdl evynftgegg valamyntde sirsfaeasm avalekkwpl ylstkntilk

241 kydgrfkdif qevyeagwks kyeaagiwye hrliddmvay alkseggyvw acknydgdvq

301 sdflaqgfgs lglmtsvlvc pdgktieaea ahgtvtrhfr vhqkggetst nsiasifawt

361 rglahrakld dnatlldfte kleaacigvv esgkmtkdla lilhgsklsr ehylnteefi

421 davaaelktk isa


LOCUS 2497258 371 aa 01-NOV-1997

DEFINITION ISOCITRATE DEHYDROGENASE (NADP) (OXALOSUCCINATE DECARBOXYLASE) (IDH) (NADP+-SPECIFIC ICDH) (IDP).

ACCESSION 2497258

PID g2497258

DB SOURCE SWISS-PROT: locus IDH_METJA, accession Q58991

class: standard.

created: Nov 1, 1997.

sequence updated: Nov 1, 1997.

annotation updated: Nov 1, 1997.

xrefs: gi: 2826435, gi: 1592206

xrefs (non-sequence databases): PROSITE PS00470, TIGR MJ1596

KEYWORDS OXIDOREDUCTASE; NADP; GLYOXYLATE BYPASS; TRICARBOXYLIC ACID CYCLE.

SOURCE Methanococcus jannaschii.

ORGANISM Methanococcus jannaschii

Archaea; Euryarchaeota; Methanococcales; Methanococcaceae;

Methanococcus.

REFERENCE 1 (residues 1 to 371)

AUTHORS BULT,C.J., WHITE,O., OLSEN,G.J., ZHOU,L., FLEISCHMANN,R.D.,

SUTTON,G.G., BLAKE,J.A., FITZGERALD,L.M., CLAYTON,R.A.,

GOCAYNE,J.D., KERLAVAGE,A.R., DOUGHERTY,B.A., TOMB,J.-F.,

ADAMS,M.D., REICH,C.I., OVERBEEK,R., KIRKNESS,E.F., WEINSTOCK,K.G.,

MERRICK,J.M., GLODEK,A., SCOTT,J.L., GEOGHAGEN,N.S.M.,

WEIDMAN,J.F., FUHRMANN,J.L., NGUYEN,D., UTTERBACK,T.R.,

KELLEY,J.M., PETERSON,J.D., SADOW,P.W., HANNA,M.C., COTTON,M.D.,

ROBERTS,K.M., HURST,M.A., KAINE,B.P., BORODOVSKY,M., KLENK,H.-P.,

FRASER,C.M., SMITH,H.O., WOESE,C.R. and VENTER,J.C.

TITLE Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii

JOURNAL Science 273 (5278), 1058-1073 (1996)

MEDLINE 96337999

REMARK SEQUENCE FROM N.A.

COMMENT [CATALYTIC ACTIVITY] ISOCITRATE + NADP(+) = 2-OXOGLUTARATE + CO(2)

+ NADPH.

[SIMILARITY] BELONGS TO THE ISOCITRATE AND ISOPROPYLMALATE

DEHYDROGENASES FAMILY.

FEATURES Location/Qualifiers

source 1..371

/organism="Methanococcus jannaschii"

/db_xref="taxon:2190"

1..371

Protein 1..371

/product="ISOCITRATE DEHYDROGENASE"

/EC_number="1.1.1.42"

Site 105

/note="BINDING TO ISOCITRATE."

/site_type="active"

ORIGIN

1 mfisywllqn vferhyikkf lvlsmmkvcv iegdgigkev ipeaxkilne lgefeiikge

61 agleclkkyg nalpedtiek akeadiilfg aitspkpgev qnykspiitl rkmfhlyanv

121 rpinnfgigq ligkiadyef lnaknidivi irentedlyv grerlendta iaervitrkg

181 seriirfafe yaiknnrkkv scihkanvlr itdglflevf neikkhynie addylvdsta

241 mnlikhpekf dvivttnmfg dilsdeasal igglglapsa nigddkalfe pvhgsapdia

301 gkgianpmas ilsiamlfdy igekekgdli reavkyclin kkvtpdlggd lktkdvgdei

361 lnyirkklkg y

 


LOCUS 2497256 393 aa 01-NOV-1997

DEFINITION ISOCITRATE DEHYDROGENASE (NADP) (OXALOSUCCINATE DECARBOXYLASE) (IDH) (NADP+-SPECIFIC ICDH) (IDP).

ACCESSION 2497256

PID g2497256

DB SOURCE SWISS-PROT: locus IDH_STRMU, accession Q59940

class: standard.

extra accessions:Q59927,created: Nov 1, 1997.

sequence updated: Nov 1, 1997.

annotation updated: Nov 1, 1997.

xrefs: gi: 1421811, gi: 1421814, gi: 1213505, gi: 1213506

xrefs (non-sequence databases): PROSITE PS00470

KEYWORDS OXIDOREDUCTASE; NADP; GLYOXYLATE BYPASS; TRICARBOXYLIC ACID CYCLE.

SOURCE Streptococcus mutans.

ORGANISM Streptococcus mutans

Eubacteria; Firmicutes; Low G+C gram-positive bacteria;

Streptococcaceae; Streptococcus.

REFERENCE 1 (residues 1 to 393)

AUTHORS CVITKOVITCH,D.G., GUTIERREZ,J.A. and BLEIWEIS,A.S.

TITLE Direct Submission

JOURNAL Submitted (??-JUL-1996) TO EMBL/GENBANK/DDBJ DATA BANKS

REMARK SEQUENCE FROM N.A.

STRAIN=JH1005

REFERENCE 2 (residues 1 to 393)

AUTHORS GUTIERREZ,J.A., CROWLEY,P.J., BROWN,D.P., HILLMAN,J.D., YOUNGMAN,P. and BLEIWEIS,A.S.

TITLE Direct Submission

JOURNAL Submitted (??-MAR-1996) TO EMBL/GENBANK/DDBJ DATA BANKS

REMARK SEQUENCE OF 66-224 FROM N.A.

STRAIN=JH1005

COMMENT [CATALYTIC ACTIVITY] ISOCITRATE + NADP(+) = 2-OXOGLUTARATE + CO(2) + NADPH.

[SUBUNIT] HOMODIMER (BY SIMILARITY).

[SIMILARITY] BELONGS TO THE ISOCITRATE AND ISOPROPYLMALATE

DEHYDROGENASES FAMILY.

FEATURES Location/Qualifiers

source 1..393

/organism="Streptococcus mutans"

/db_xref="taxon:1309"

1..393

Protein 1..393

/product="ISOCITRATE DEHYDROGENASE"

/EC_number="1.1.1.42"

Region 67

/note="K -> N (IN REF. 2)."

/region_name="Conflict"

Site 102

/note="BINDING TO ISOCITRATE."

/site_type="active"

ORIGIN

1 maekvsfeeg klqvpdkpvi pyiegdgvgq diwknaqivf dkaiakvygg hkqviwrevl

61 agkkayketg nwlpnetlei ikthllaikg pletpvgggi rslnvalrqe ldlfacvrpv

121 ryfkgvpspl khpektaiti frentediya giewnagtae vqkvinflqd dmqvkkirfp

181 ksssigikpi siegsqrlir aaieyalann ltkvtlvhkg niqkfteggf rkwgyelakr

241 eyaaelasgq lvvddiiadn flqqillkpe rfdvvaltnl ngdyasdala aqvggigisp

301 ganinyqtgh aifeathgta pdiagqdlan pssvllsgcm lfdyigwskv sdlimkavek

361 aiangqvtid fakelgveal ttcqfsevll tyl


LOCUS 2497257 391 aa 01-NOV-1997

DEFINITION ISOCITRATE DEHYDROGENASE (NADP) (OXALOSUCCINATE DECARBOXYLASE)

(IDH) (NADP+-SPECIFIC ICDH) (IDP).

ACCESSION 2497257

PID g2497257

DB SOURCE SWISS-PROT: locus IDH_STRSL, accession Q59985

class: standard.

created: Nov 1, 1997.

sequence updated: Nov 1, 1997.

annotation updated: Nov 1, 1997.

xrefs: gi: 1280401, gi: 1280403

xrefs (non-sequence databases): PROSITE PS00470

KEYWORDS OXIDOREDUCTASE; NADP; GLYOXYLATE BYPASS; TRICARBOXYLIC ACID CYCLE.

SOURCE Streptococcus salivarius.

ORGANISM Streptococcus salivarius

Eubacteria; Firmicutes; Low G+C gram-positive bacteria;

Streptococcaceae; Streptococcus.

REFERENCE 1 (residues 1 to 391)

AUTHORS DESGAGNES,R., GAGNON,G. and FRENETTE,M.

TITLE Direct Submission

JOURNAL Submitted (??-APR-1996) TO EMBL/GENBANK/DDBJ DATA BANKS

REMARK SEQUENCE FROM N.A.

STRAIN=ATCC 25975

COMMENT [CATALYTIC ACTIVITY] ISOCITRATE + NADP(+) = 2-OXOGLUTARATE + CO(2)

+ NADPH.

[SUBUNIT] HOMODIMER (BY SIMILARITY).

[SIMILARITY] BELONGS TO THE ISOCITRATE AND ISOPROPYLMALATE

DEHYDROGENASES FAMILY.

FEATURES Location/Qualifiers

source 1..391

/organism="Streptococcus salivarius"

/db_xref="taxon:1304"

1..391

Protein 1..391

/product="ISOCITRATE DEHYDROGENASE"

/EC_number="1.1.1.42"

Site 102

/note="BINDING TO ISOCITRATE."

/site_type="active"

ORIGIN

1 maekivmkng qlqvsdrpii pfiegdgvgh diwknaqaif dkavevayeg krhiewqell

61 agkkaydktg ewlpketlea ireslvaikg pletpvgggi rslnvalrqe ldlyacvrpv

121 ryfdgvaspl kepektniti frentediya gieweagtad vkrvieflqt emnvnkirfp

181 esssigikpi siegskrlir saidyalknn lkkvtlvhkg niqkfteggf rkwgyevaqe

241 dykeellagr leindiiadn flqqillnpe kfdvvaltnl ngdyasdala aqvggigisp

301 ganinyqtgh aifeathgta pdiadqdkan pcsvllsgcm lldyigwtea aqlitsaiek

361 tfkadiftad lafgkqayst safsnqilsi m


LOCUS 124171 416 aa 01-FEB-1998

DEFINITION ISOCITRATE DEHYDROGENASE (NADP) (OXALOSUCCINATE DECARBOXYLASE) (IDH) (NADP+-SPECIFIC ICDH) (IDP).

ACCESSION 124171

PID g124171

DB SOURCE SWISS-PROT: locus IDH_ECOLI, accession P08200

class: standard.

created: Aug 1, 1988.

sequence updated: Aug 1, 1988.

annotation updated: Feb 1, 1998.

xrefs: gi: 146431, gi: 146432, gi: 1787371, gi: 1787381, gi:

1651553, gi: 1651560, gi: 1651562, gi: 1651566, gi: 65942

xrefs (non-sequence databases): SWISS-2DPAGE P08200, ECO2DBASE

C043.8, ECOGENE EG10489, ECOGENE EG10009, PROSITE PS00470

KEYWORDS OXIDOREDUCTASE; NADP; PHOSPHORYLATION; GLYOXYLATE BYPASS; TRICARBOXYLIC ACID CYCLE; 3D-STRUCTURE.

SOURCE Escherichia coli.

ORGANISM Escherichia coli

Eubacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae;

Escherichia.

REFERENCE 1 (residues 1 to 416)

AUTHORS Thorsness,P.E. and Koshland,D.E. Jr.

TITLE Inactivation of isocitrate dehydrogenase by phosphorylation is mediated by the negative charge of the phosphate

JOURNAL J. Biol. Chem. 262 (22), 10422-10425 (1987)

MEDLINE 87280090

REMARK SEQUENCE FROM N.A.

REFERENCE 2 (residues 1 to 416)

AUTHORS BLATTNER,F.R., PLUNKETT,G. III, MAYHEW,G.F., PERNA,N.T. and GLASNER,F.D.

TITLE Direct Submission

JOURNAL Submitted (??-JAN-1997) TO EMBL/GENBANK/DDBJ DATA BANKS

REMARK SEQUENCE FROM N.A.

STRAIN=K12 / MG1655

REFERENCE 3 (residues 1 to 416)

AUTHORS OSHIMA,T., AIBA,H., BABA,T., FUJITA,K., HAYASHI,K., HONJO,A.,

IKEMOTO,K., INADA,T., ITOH,T., KAJIHARA,M., KANAI,K., KASHIMOTO,K.,

KIMURA,S., KITAGAWA,M., MAKINO,K., MASUDA,S., MIKI,T.,

MIZOBUCHI,K., MORI,H., MOTOMURA,K., NAKAMURA,Y., NASHIMOTO,H.,

NISHIO,Y., SAITO,N., SAMPEI,G., SEKI,Y., TAGAMI,H., TAKEMOTO,K.,

WADA,C., YAMAMOTO,Y., YANO,M. and HORIUCHI,T.

TITLE A 718-kb DNA sequence of the Escherichia coli K-12 genome

corresponding to the 12.7-28.0 min region on the linkage map

JOURNAL DNA Res. 3 (3), 137-155 (1996)

MEDLINE 97061202

REMARK SEQUENCE FROM N.A.

STRAIN=K12

REFERENCE 4 (residues 1 to 416)

AUTHORS LINK,A.J.

TITLE Direct Submission

JOURNAL Submitted (??-OCT-1994) TO THE SWISS-PROT DATA BANK

REMARK SEQUENCE OF 1-12.

STRAIN=K12 / EMG2

REFERENCE 5 (residues 1 to 416)

AUTHORS Hurley,J.H., Thorsness,P.E., Ramalingam,V., Helmers,N.H.,

Koshland,D.E. Jr. and Stroud,R.M.

TITLE Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase

JOURNAL Proc. Natl. Acad. Sci. U.S.A. 86 (22), 8635-8639 (1989)

MEDLINE 90046847

REMARK X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

REFERENCE 6 (residues 1 to 416)

AUTHORS Hurley,J.H., Dean,A.M., Sohl,J.L., Koshland,D.E. Jr. and

Stroud,R.M.

TITLE Regulation of an enzyme by phosphorylation at the active site

JOURNAL Science 249 (4972), 1012-1016 (1990)

MEDLINE 90371294

REMARK INFLUENCE OF PHOSPHORYLATION.

COMMENT [CATALYTIC ACTIVITY] ISOCITRATE + NADP(+) = 2-OXOGLUTARATE + CO(2)

+ NADPH.

[ENZYME REGULATION] INHIBITION OF THIS ENZYME BY PHOSPHORYLATION

REGULATES THE BRANCH POINT BETWEEN THE KREBS CYCLE AND THE

GLYOXYLATE BYPASS, WHICH IS AN ALTERNATE ROUTE THAT ACCUMULATES

CARBON FOR BIOSYNTHESIS WHEN ACETATE IS THE SOLE CARBON SOURCE FOR

GROWTH.

[SUBUNIT] HOMODIMER.

[PTM] PHOSPHORYLATION STATE OF THIS ENZYME IS CONTROLLED BY

ISOCITRATE DEHYDROGENASE KINASE/PHOSPHATASE (ACEK).

[SIMILARITY] BELONGS TO THE ISOCITRATE AND ISOPROPYLMALATE

DEHYDROGENASES FAMILY.

FEATURES Location/Qualifiers

source 1..416

/organism="Escherichia coli"

/db_xref="taxon:562"

1..416

Protein 1..416

/product="ISOCITRATE DEHYDROGENASE"

/EC_number="1.1.1.42"

Region 12

/region_name="Beta-strand region"

Region 15..17

/region_name="Beta-strand region"

Region 18..19

/region_name="Hydrogen bonded turn"

Region 20..22

/region_name="Beta-strand region"

Region 27..32

/region_name="Beta-strand region"

Region 36..37

/region_name="Hydrogen bonded turn"

Region 38..57

/region_name="Helical region"

Region 58..59

/region_name="Hydrogen bonded turn"

Region 64..68

/region_name="Beta-strand region"

Region 71

/region_name="Hydrogen bonded turn"

Region 72..78

/region_name="Helical region"

Region 80..81

/region_name="Hydrogen bonded turn"

Region 86..95

/region_name="Helical region"

Region 97..100

/region_name="Beta-strand region"

Site 113

/note="BINDING TO ISOCITRATE."

/site_type="active"

Site 113

/site_type="phosphorylation"

Region 114..121

/region_name="Helical region"

Region 122..123

/region_name="Hydrogen bonded turn"

Region 126..132

/region_name="Beta-strand region"

Region 135..136

/region_name="Hydrogen bonded turn"

Region 144..146

/region_name="Helical region"

Region 148..154

/region_name="Beta-strand region"

Region 159..161

/region_name="Helical region"

Region 164..165

/region_name="Beta-strand region"

Region 167..168

/region_name="Hydrogen bonded turn"

Region 170..181

/region_name="Helical region"

Region 182

/region_name="Hydrogen bonded turn"

Region 192..193

/region_name="Hydrogen bonded turn"

Region 196..197

/region_name="Beta-strand region"

Region 203..219

/region_name="Helical region"

Region 220..221

/region_name="Hydrogen bonded turn"

Region 224..229

/region_name="Beta-strand region"

Region 231..233

/region_name="Hydrogen bonded turn"

Region 235..237

/region_name="Hydrogen bonded turn"

Region 238..253

/region_name="Helical region"

Region 256..257

/region_name="Beta-strand region"

Region 259..260

/region_name="Hydrogen bonded turn"

Region 264..267

/region_name="Beta-strand region"

Region 269..271

/region_name="Hydrogen bonded turn"

Region 274..281

/region_name="Beta-strand region"

Region 282..291

/region_name="Helical region"

Region 293..295

/region_name="Helical region"

Region 298..301

/region_name="Beta-strand region"

Region 303..316

/region_name="Helical region"

Region 317..318

/region_name="Hydrogen bonded turn"

Region 320..322

/region_name="Hydrogen bonded turn"

Region 324..328

/region_name="Beta-strand region"

Region 333..337

/region_name="Beta-strand region"

Region 343..347

/region_name="Hydrogen bonded turn"

Region 353

/region_name="Hydrogen bonded turn"

Region 354..366

/region_name="Helical region"

Region 367..368

/region_name="Hydrogen bonded turn"

Region 370..385

/region_name="Helical region"

Region 386..387

/region_name="Hydrogen bonded turn"

Region 388..390

/region_name="Beta-strand region"

Region 391..394

/region_name="Helical region"

Region 395..396

/region_name="Hydrogen bonded turn"

Region 401..403

/region_name="Beta-strand region"

Region 405..414

/region_name="Helical region"

Region 415

/region_name="Hydrogen bonded turn"

ORIGIN

1 meskvvvpaq gkkitlqngk lnvpenpiip yiegdgigvd vtpamlkvvd aavekaykge

61 rkiswmeiyt gekstqvygq dvwlpaetld lireyrvaik gplttpvggg irslnvalrq

121 eldlyiclrp vryyqgtpsp vkhpeltdmv ifrensediy agiewkadsa daekvikflr

181 eemgvkkirf pehcgigikp cseegtkrlv raaieyaian drdsvtlvhk gnimkftega

241 fkdwgyqlar eefggelidg gpwlkvknpn tgkeivikdv iadaflqqil lrpaeydvia

301 cmnlngdyis dalaaqvggi giapganigd ecalfeathg tapkyagqdk vnpgsiilsa

361 emmlrhmgwt eaadlivkgm egainaktvt ydferlmdga kllkcsefgd aiienm