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P31002 (IMDH_ACICA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 86. 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
OrganismAcinetobacter calcoaceticus
Taxonomic identifier471 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex

Protein attributes

Sequence length488 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.

Ontologies

Keywords
   Biological processGMP biosynthesis
Purine biosynthesis
   DomainCBS domain
Repeat
   LigandMetal-binding
NAD
Potassium
   Molecular functionOxidoreductase
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 – 488488Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964
PRO_0000093688

Regions

Domain93 – 14856CBS 1
Domain152 – 21059CBS 2
Nucleotide binding297 – 2993NAD By similarity
Region336 – 3383IMP binding By similarity
Region359 – 3602IMP binding By similarity
Region383 – 3875IMP binding By similarity

Sites

Active site3041Thioimidate intermediate By similarity
Metal binding2991Potassium; via carbonyl oxygen By similarity
Metal binding3011Potassium; via carbonyl oxygen By similarity
Metal binding3041Potassium; via carbonyl oxygen By similarity
Metal binding4701Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4711Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4721Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site2471NAD By similarity
Binding site3021IMP By similarity
Binding site4161IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
P31002 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 3DE0F8F9B5157A03

FASTA48851,530
        10         20         30         40         50         60 
MLTIVQEALT FDDVLLLPAY STVLPKDVSL KTRLTRGIYL NIPLVSAAMD TVTESRMAIA 

        70         80         90        100        110        120 
MAQNGGIGIL HKNMDIAAQA AEVRRVKKFE AGMVKDPITV SPETTVRELI AITSANNISG 

       130        140        150        160        170        180 
VPVVKDSKVV GIVTGRDTRF ETNLEQPVSN IMTGQDRLVT VREGESKENI QALLQKHRIE 

       190        200        210        220        230        240 
KVLVVGESNE LKGLITVTDF RKAESYPNSC KDDLGRLRVG AAVGTGADTP SRVEALVEAG 

       250        260        270        280        290        300 
VDVIVVDTAH GHSAGVIERV RWVKQNFPQV QVIGGNIATG DAALALLDAG ADAVKVGIGP 

       310        320        330        340        350        360 
GSICTTRIVA GIGMPQISAI DSVASALKDQ IPLIADGGIP FSGDMAKAIG AGASTIMVGS 

       370        380        390        400        410        420 
LLAGTEEAPG EVEFFQGRYY KAYRGMGSLG AMAGRTGSAD RYFQDSKAGA EKLVPEGIEG 

       430        440        450        460        470        480 
RVPYKGPMGN IVHQMMGGLR SSMGYTGSAV IEDLRQNAKF VKITSAGMSE SHVHDVTITK 


EAPNYRVG 

« Hide

References

[1]Anderegg U., Schnuck W.H., Asperger O., Kleber H.-P.
Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: EB 104.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X66859 Genomic DNA. Translation: CAA47328.1.
PIRS23226.

3D structure databases

ProteinModelPortalP31002.
SMRP31002. Positions 4-486.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP31002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

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_ACICA
AccessionPrimary (citable) accession number: P31002
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: February 19, 2014
This is version 86 of the entry and version 1 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