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P39126

- IDH_BACSU

UniProt

P39126 - IDH_BACSU

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Protein

Isocitrate dehydrogenase [NADP]

Gene
icd, citC, BSU29130
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

Isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH.

Cofactori

Binds 1 magnesium or manganese ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei95 – 951NADP By similarity
Binding sitei96 – 961Substrate
Binding sitei104 – 1041Substrate
Binding sitei106 – 1061Substrate
Binding sitei110 – 1101Substrate
Binding sitei120 – 1201Substrate By similarity
Binding sitei144 – 1441Substrate
Sitei151 – 1511Critical for catalysis By similarity
Sitei221 – 2211Critical for catalysis By similarity
Metal bindingi311 – 3111Magnesium or manganese By similarity
Binding sitei358 – 3581NADP; via amide nitrogen and carbonyl oxygen By similarity
Binding sitei397 – 3971NADP By similarity
Binding sitei401 – 4011NADP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi345 – 3517NADP By similarity

GO - Molecular functioni

  1. isocitrate dehydrogenase (NADP+) activity Source: UniProtKB-EC
  2. magnesium ion binding Source: InterPro
  3. NAD binding Source: InterPro
  4. protein binding Source: IntAct

GO - Biological processi

  1. glyoxylate cycle Source: UniProtKB-KW
  2. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glyoxylate bypass, Tricarboxylic acid cycle

Keywords - Ligandi

Magnesium, Manganese, Metal-binding, NADP

Enzyme and pathway databases

BioCyciBSUB:BSU29130-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Isocitrate dehydrogenase [NADP] (EC:1.1.1.42)
Short name:
IDH
Alternative name(s):
IDP
NADP(+)-specific ICDH
Oxalosuccinate decarboxylase
Gene namesi
Name:icd
Synonyms:citC
Ordered Locus Names:BSU29130
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU29130. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 423423Isocitrate dehydrogenase [NADP]PRO_0000083549Add
BLAST

Proteomic databases

PaxDbiP39126.
PRIDEiP39126.

PTM databases

PhosSiteiP0204106.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
mdhP498143EBI-7829570,EBI-7827708

Protein-protein interaction databases

IntActiP39126. 2 interactions.
MINTiMINT-1711252.
STRINGi224308.BSU29130.

Structurei

Secondary structure

1
423
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53
Beta strandi8 – 103
Beta strandi13 – 153
Beta strandi18 – 258
Helixi31 – 5020
Beta strandi57 – 604
Helixi65 – 717
Helixi77 – 8610
Beta strandi88 – 914
Beta strandi98 – 1025
Helixi105 – 1128
Beta strandi117 – 1237
Beta strandi131 – 1333
Helixi135 – 1373
Beta strandi139 – 1457
Helixi149 – 1524
Helixi161 – 17313
Helixi182 – 1843
Beta strandi185 – 1939
Helixi194 – 21118
Beta strandi214 – 2207
Turni222 – 2243
Turni226 – 2283
Helixi229 – 24416
Helixi245 – 2473
Beta strandi248 – 2503
Helixi251 – 27525
Beta strandi279 – 2857
Helixi286 – 29510
Helixi297 – 2993
Beta strandi301 – 3055
Helixi307 – 32014
Turni324 – 3263
Beta strandi328 – 3325
Turni334 – 3363
Beta strandi339 – 3446
Helixi349 – 3513
Turni352 – 3554
Helixi360 – 37314
Helixi376 – 39116
Helixi397 – 4004
Beta strandi403 – 4053
Helixi411 – 42010

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HQSX-ray1.55A/B1-423[»]
ProteinModelPortaliP39126.
SMRiP39126. Positions 1-423.

Miscellaneous databases

EvolutionaryTraceiP39126.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0538.
HOGENOMiHOG000021113.
KOiK00031.
OMAiCLRPIRY.
OrthoDBiEOG6SNDTP.
PhylomeDBiP39126.

Family and domain databases

Gene3Di3.40.718.10. 1 hit.
InterProiIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR004439. Isocitrate_DH_NADP_dimer_prok.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
PANTHERiPTHR11835. PTHR11835. 1 hit.
PfamiPF00180. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00183. prok_nadp_idh. 1 hit.
PROSITEiPS00470. IDH_IMDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39126-1 [UniParc]FASTAAdd to Basket

« Hide

MAQGEKITVS NGVLNVPNNP IIPFIEGDGT GPDIWNAASK VLEAAVEKAY    50
KGEKKITWKE VYAGEKAYNK TGEWLPAETL DVIREYFIAI KGPLTTPVGG 100
GIRSLNVALR QELDLFVCLR PVRYFTGVPS PVKRPEDTDM VIFRENTEDI 150
YAGIEYAKGS EEVQKLISFL QNELNVNKIR FPETSGIGIK PVSEEGTSRL 200
VRAAIDYAIE HGRKSVTLVH KGNIMKFTEG AFKNWGYELA EKEYGDKVFT 250
WAQYDRIAEE QGKDAANKAQ SEAEAAGKII IKDSIADIFL QQILTRPNEF 300
DVVATMNLNG DYISDALAAQ VGGIGIAPGA NINYETGHAI FEATHGTAPK 350
YAGLDKVNPS SVILSGVLLL EHLGWNEAAD LVIKSMEKTI ASKVVTYDFA 400
RLMDGATEVK CSEFGEELIK NMD 423
Length:423
Mass (Da):46,418
Last modified:February 1, 1995 - v1
Checksum:iCC69E694EB66D0D8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U05257 Genomic DNA. Translation: AAA96342.1.
AF008220 Genomic DNA. Translation: AAC00346.1.
AL009126 Genomic DNA. Translation: CAB14873.1.
PIRiI40382.
RefSeqiNP_390791.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB14873; CAB14873; BSU29130.
GeneIDi938183.
KEGGibsu:BSU29130.
PATRICi18977720. VBIBacSub10457_3048.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U05257 Genomic DNA. Translation: AAA96342.1 .
AF008220 Genomic DNA. Translation: AAC00346.1 .
AL009126 Genomic DNA. Translation: CAB14873.1 .
PIRi I40382.
RefSeqi NP_390791.1. NC_000964.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HQS X-ray 1.55 A/B 1-423 [» ]
ProteinModelPortali P39126.
SMRi P39126. Positions 1-423.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P39126. 2 interactions.
MINTi MINT-1711252.
STRINGi 224308.BSU29130.

PTM databases

PhosSitei P0204106.

Proteomic databases

PaxDbi P39126.
PRIDEi P39126.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB14873 ; CAB14873 ; BSU29130 .
GeneIDi 938183.
KEGGi bsu:BSU29130.
PATRICi 18977720. VBIBacSub10457_3048.

Organism-specific databases

GenoListi BSU29130. [Micado ]

Phylogenomic databases

eggNOGi COG0538.
HOGENOMi HOG000021113.
KOi K00031.
OMAi CLRPIRY.
OrthoDBi EOG6SNDTP.
PhylomeDBi P39126.

Enzyme and pathway databases

BioCyci BSUB:BSU29130-MONOMER.

Miscellaneous databases

EvolutionaryTracei P39126.

Family and domain databases

Gene3Di 3.40.718.10. 1 hit.
InterProi IPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR004439. Isocitrate_DH_NADP_dimer_prok.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view ]
PANTHERi PTHR11835. PTHR11835. 1 hit.
Pfami PF00180. Iso_dh. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00183. prok_nadp_idh. 1 hit.
PROSITEi PS00470. IDH_IMDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of two distinct Bacillus subtilis citrate synthase genes."
    Jin S., Sonenshein A.L.
    J. Bacteriol. 176:4669-4679(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / SMY.
  2. "Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region."
    Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.
    Microbiology 143:3431-3441(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  4. "Bacillus subtilis isocitrate dehydrogenase. A substrate analogue for Escherichia coli isocitrate dehydrogenase kinase/phosphatase."
    Singh S.K., Miller S.P., Dean A., Banaszak L.J., LaPorte D.C.
    J. Biol. Chem. 277:7567-7573(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  5. "Crystal structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 A. Insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphatase."
    Singh S.K., Matsuno K., LaPorte D.C., Banaszak L.J.
    J. Biol. Chem. 276:26154-26163(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH CITRATE, SUBUNIT.

Entry informationi

Entry nameiIDH_BACSU
AccessioniPrimary (citable) accession number: P39126
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The enzyme can be phosphorylated in vitro by the E.coli isocitrate dehydrogenase kinase/phosphatase, but B.subtilis lacks such an enzyme.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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