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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Chlorobaculum parvum (strain NCIB 8327) (Chlorobium vibrioforme subsp. thiosulfatophilum (strain DSM 263 / NCIB 8327))
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.UniRule annotation

Catalytic activityi

Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH.UniRule annotation

Cofactori

K+UniRule annotation

Enzyme regulationi

Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH.UniRule annotation

Pathwayi: XMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes XMP from IMP.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Inosine-5'-monophosphate dehydrogenase (guaB)
This subpathway is part of the pathway XMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes XMP from IMP, the pathway XMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei251NADUniRule annotation1
Metal bindingi303Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi305Potassium; via carbonyl oxygenUniRule annotation1
Binding sitei306IMPUniRule annotation1
Active sitei308Thioimidate intermediateUniRule annotation1
Metal bindingi308Potassium; via carbonyl oxygenUniRule annotation1
Active sitei406Proton acceptorUniRule annotation1
Binding sitei421IMPUniRule annotation1
Metal bindingi475Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi476Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi477Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi301 – 303NADUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

GMP biosynthesis, Purine biosynthesis

Keywords - Ligandi

Metal-binding, NAD, Potassium

Enzyme and pathway databases

UniPathwayiUPA00601; UER00295.

Names & Taxonomyi

Protein namesi
Recommended name:
Inosine-5'-monophosphate dehydrogenaseUniRule annotation (EC:1.1.1.205UniRule annotation)
Short name:
IMP dehydrogenaseUniRule annotation
Short name:
IMPDUniRule annotation
Short name:
IMPDHUniRule annotation
Gene namesi
Name:guaBUniRule annotation
Ordered Locus Names:Cpar_0730
OrganismiChlorobaculum parvum (strain NCIB 8327) (Chlorobium vibrioforme subsp. thiosulfatophilum (strain DSM 263 / NCIB 8327))
Taxonomic identifieri517417 [NCBI]
Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum
Proteomesi
  • UP000008811 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000936941 – 494Inosine-5'-monophosphate dehydrogenaseAdd BLAST494

Proteomic databases

PRIDEiO50316.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi517417.Cpar_0730.

Structurei

3D structure databases

ProteinModelPortaliO50316.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini93 – 154CBS 1UniRule annotationAdd BLAST62
Domaini158 – 217CBS 2UniRule annotationAdd BLAST60

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni341 – 343IMP bindingUniRule annotation3
Regioni364 – 365IMP bindingUniRule annotation2
Regioni388 – 392IMP bindingUniRule annotation5

Sequence similaritiesi

Belongs to the IMPDH/GMPR family.UniRule annotation
Contains 2 CBS domains.UniRule annotation

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiENOG4105CP4. Bacteria.
COG0516. LUCA.
COG0517. LUCA.
HOGENOMiHOG000165755.
KOiK00088.
OMAiSSMGYCG.
OrthoDBiPOG091H02IM.

Family and domain databases

CDDicd00381. IMPDH. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PANTHERiPTHR11911:SF6. PTHR11911:SF6. 2 hits.
PfamiPF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFiPIRSF000130. IMPDH. 1 hit.
SMARTiSM00116. CBS. 2 hits.
[Graphical view]
TIGRFAMsiTIGR01302. IMP_dehydrog. 1 hit.
PROSITEiPS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O50316-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDKILYDALT FDDVLLVPAY SNVLPKETVV KSRVTRNIEV NLPLVSAAMD
60 70 80 90 100
TVTEAELAIA LARAGGIGII HKNLSIDVQA RHVAKVKRFE SGIIRNPITL
110 120 130 140 150
FEDATIQEAI DLMLRHSISG IPVVERPTPE GCLLLKGIVT NRDLRMTTSS
160 170 180 190 200
NEKITTIMTT DLITAQEDID LLAAEEILMQ NKIEKLLVID EEGYLKGLIT
210 220 230 240 250
FKDIQKRKQC PDACKDMHGR LRVGAAVGIR SNTITRVDAL VEAGVDVVAV
260 270 280 290 300
DTAHGHSQAV LDMVATIKEK YPELEVIAGN VATPEAVRDL VKAGADAVKV
310 320 330 340 350
GIGPGSICTT RVVAGVGMPQ LTAIMNCAKE AAKTDTPIIA DGGIKYSGDI
360 370 380 390 400
SKALAAGADT VMMGSIFAGT DESPGETILY EGRRFKAYRG MGSLGAMSEP
410 420 430 440 450
EGSSDRYFQD ASAETKKYVP EGIEGRIPAK GPLDEVVYQL IGGLKSSMGY
460 470 480 490
CGVKNIEELK KNTRFVRITS AGLRESHPHD VMITREAPNY STSH
Length:494
Mass (Da):53,202
Last modified:October 14, 2008 - v3
Checksum:iE920D6B0B60C44AC
GO

Sequence cautioni

The sequence CAB06303 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti158M → I in CAB06303 (Ref. 1) Curated1
Sequence conflicti429 – 431AKG → QR in CAB06303 (Ref. 1) Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z83933 Genomic DNA. Translation: CAB06303.1. Different initiation.
CP001099 Genomic DNA. Translation: ACF11149.1.
PIRiT17196.
RefSeqiWP_012501982.1. NC_011027.1.

Genome annotation databases

EnsemblBacteriaiACF11149; ACF11149; Cpar_0730.
KEGGicpc:Cpar_0730.
PATRICi21364712. VBIChlPar72705_0729.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z83933 Genomic DNA. Translation: CAB06303.1. Different initiation.
CP001099 Genomic DNA. Translation: ACF11149.1.
PIRiT17196.
RefSeqiWP_012501982.1. NC_011027.1.

3D structure databases

ProteinModelPortaliO50316.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi517417.Cpar_0730.

Proteomic databases

PRIDEiO50316.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACF11149; ACF11149; Cpar_0730.
KEGGicpc:Cpar_0730.
PATRICi21364712. VBIChlPar72705_0729.

Phylogenomic databases

eggNOGiENOG4105CP4. Bacteria.
COG0516. LUCA.
COG0517. LUCA.
HOGENOMiHOG000165755.
KOiK00088.
OMAiSSMGYCG.
OrthoDBiPOG091H02IM.

Enzyme and pathway databases

UniPathwayiUPA00601; UER00295.

Family and domain databases

CDDicd00381. IMPDH. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PANTHERiPTHR11911:SF6. PTHR11911:SF6. 2 hits.
PfamiPF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFiPIRSF000130. IMPDH. 1 hit.
SMARTiSM00116. CBS. 2 hits.
[Graphical view]
TIGRFAMsiTIGR01302. IMP_dehydrog. 1 hit.
PROSITEiPS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIMDH_CHLP8
AccessioniPrimary (citable) accession number: O50316
Secondary accession number(s): B3QMJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: October 14, 2008
Last modified: November 2, 2016
This is version 107 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.