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