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O50316 (IMDH_CHLP8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inosine-5'-monophosphate dehydrogenase

Short name=IMP dehydrogenase
Short name=IMPD
Short name=IMPDH
EC=1.1.1.205
Gene names
Name:guaB
Ordered Locus Names:Cpar_0730
OrganismChlorobaculum parvum (strain NCIB 8327) (Chlorobium vibrioforme subsp. thiosulfatophilum (strain DSM 263 / NCIB 8327)) [Complete proteome] [HAMAP]
Taxonomic identifier517417 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_01964

Catalytic activity

Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH. HAMAP-Rule MF_01964

Cofactor

Potassium By similarity. HAMAP-Rule MF_01964

Enzyme regulation

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 By similarity. HAMAP-Rule MF_01964

Pathway

Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. HAMAP-Rule MF_01964

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_01964

Sequence similarities

Belongs to the IMPDH/GMPR family.

Contains 2 CBS domains.

Sequence caution

The sequence CAB06303.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processGMP biosynthesis
Purine biosynthesis
   DomainCBS domain
Repeat
   LigandMetal-binding
NAD
Potassium
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processGMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionIMP dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

adenyl nucleotide binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 494494Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964
PRO_0000093694

Regions

Domain93 – 15462CBS 1
Domain158 – 21760CBS 2
Nucleotide binding301 – 3033NAD By similarity
Region341 – 3433IMP binding By similarity
Region364 – 3652IMP binding By similarity
Region388 – 3925IMP binding By similarity

Sites

Active site3081Thioimidate intermediate By similarity
Metal binding3031Potassium; via carbonyl oxygen By similarity
Metal binding3051Potassium; via carbonyl oxygen By similarity
Metal binding3081Potassium; via carbonyl oxygen By similarity
Metal binding4751Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4761Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4771Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site2511NAD By similarity
Binding site3061IMP By similarity
Binding site4211IMP By similarity

Experimental info

Sequence conflict1581M → I in CAB06303. Ref.1
Sequence conflict429 – 4313AKG → QR in CAB06303. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O50316 [UniParc].

Last modified October 14, 2008. Version 3.
Checksum: E920D6B0B60C44AC

FASTA49453,202
        10         20         30         40         50         60 
MDKILYDALT FDDVLLVPAY SNVLPKETVV KSRVTRNIEV NLPLVSAAMD TVTEAELAIA 

        70         80         90        100        110        120 
LARAGGIGII HKNLSIDVQA RHVAKVKRFE SGIIRNPITL FEDATIQEAI DLMLRHSISG 

       130        140        150        160        170        180 
IPVVERPTPE GCLLLKGIVT NRDLRMTTSS NEKITTIMTT DLITAQEDID LLAAEEILMQ 

       190        200        210        220        230        240 
NKIEKLLVID EEGYLKGLIT FKDIQKRKQC PDACKDMHGR LRVGAAVGIR SNTITRVDAL 

       250        260        270        280        290        300 
VEAGVDVVAV DTAHGHSQAV LDMVATIKEK YPELEVIAGN VATPEAVRDL VKAGADAVKV 

       310        320        330        340        350        360 
GIGPGSICTT RVVAGVGMPQ LTAIMNCAKE AAKTDTPIIA DGGIKYSGDI SKALAAGADT 

       370        380        390        400        410        420 
VMMGSIFAGT DESPGETILY EGRRFKAYRG MGSLGAMSEP EGSSDRYFQD ASAETKKYVP 

       430        440        450        460        470        480 
EGIEGRIPAK GPLDEVVYQL IGGLKSSMGY CGVKNIEELK KNTRFVRITS AGLRESHPHD 

       490 
VMITREAPNY STSH 

« Hide

References

« Hide 'large scale' references
[1]"Clustering of genes with function in the biosynthesis of bacteriochlorophyll and heme in the green sulfur bacterium Chlorobium vibrioforme."
Petersen B.L., Moeller M.G., Stummann B.M., Henningsen K.W.
Hereditas 125:93-96(1996)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of Chlorobaculum parvum NCIB 8327."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Zhao F., Li T., Liu Z. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCIB 8327.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z83933 Genomic DNA. Translation: CAB06303.1. Different initiation.
CP001099 Genomic DNA. Translation: ACF11149.1.
PIRT17196.
RefSeqYP_001998349.1. NC_011027.1.

3D structure databases

ProteinModelPortalO50316.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING517417.Cpar_0730.

Proteomic databases

PRIDEO50316.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF11149; ACF11149; Cpar_0730.
GeneID6419655.
KEGGcpc:Cpar_0730.
PATRIC21364712. VBIChlPar72705_0729.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0517.
HOGENOMHOG000165755.
KOK00088.
OMASSMGYCG.
OrthoDBEOG6GTZPV.
ProtClustDBCLSK637688.

Enzyme and pathway databases

BioCycCPAR517417:GH95-756-MONOMER.
UniPathwayUPA00601; UER00295.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01964. IMPDH.
InterProIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PANTHERPTHR11911:SF6. PTHR11911:SF6. 1 hit.
PfamPF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFPIRSF000130. IMPDH. 1 hit.
SMARTSM00116. CBS. 2 hits.
[Graphical view]
TIGRFAMsTIGR01302. IMP_dehydrog. 1 hit.
PROSITEPS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIMDH_CHLP8
AccessionPrimary (citable) accession number: O50316
Secondary accession number(s): B3QMJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: October 14, 2008
Last modified: February 19, 2014
This is version 93 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways