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Q9HQU4 (IMDH_HALSA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 84. 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:VNG_1001G
OrganismHalobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium) [Reference proteome] [HAMAP]
Taxonomic identifier64091 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHalobacterium

Protein attributes

Sequence length499 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 AAG19418.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processGMP biosynthesis
Purine biosynthesis
   DomainCBS domain
Repeat
   LigandMetal-binding
NAD
Potassium
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference 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 – 499499Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964
PRO_0000415692

Regions

Domain106 – 16560CBS 1
Domain169 – 22557CBS 2
Nucleotide binding308 – 3103NAD By similarity
Region348 – 3503IMP binding By similarity
Region371 – 3722IMP binding By similarity
Region395 – 3995IMP binding By similarity

Sites

Active site3151Thioimidate intermediate By similarity
Metal binding3101Potassium; via carbonyl oxygen By similarity
Metal binding3121Potassium; via carbonyl oxygen By similarity
Metal binding3151Potassium; via carbonyl oxygen By similarity
Metal binding4791Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4801Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4811Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site2601NAD By similarity
Binding site3131IMP By similarity
Binding site4251IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HQU4 [UniParc].

Last modified April 3, 2013. Version 2.
Checksum: 3A6C3B23A42B9D39

FASTA49952,767
        10         20         30         40         50         60 
MANDSSTDGR FSEKLRVPEA LTFDDVLLRP AESRVEPDDA DVATRVSTNV ELEVPVLSAA 

        70         80         90        100        110        120 
MDTVTESRLA IAMAREGGLG VLHQNMDTDR VVAEVERVKR ADELVIDREN VVTAAPEQTV 

       130        140        150        160        170        180 
EAVDEMMDRS DVSGAPVVDD DDTVRGIISA TDIRPYLEVG ESDAVREAMT DEVITAPEDI 

       190        200        210        220        230        240 
TARDALELMY EHKIERVPIV NDEQHLVGLV TMQGILERRE HGSAARDQNG RLRVGVAVGP 

       250        260        270        280        290        300 
FDTERATAVD EAGADVLFID CAHAHNLNVI DSAREIKASV DADVVVGNVG TREAAEAVVD 

       310        320        330        340        350        360 
FADGIKVGIG PGSICTTRVV TGSGMPQITA VSQVADVAAP AGVPVIADGG IRYSGDAAKA 

       370        380        390        400        410        420 
IAAGADAVML GSYFAGTDEA PGRVITMNGK KYKQYRGMGS VGAMQSGGSD RYLKDDDEDE 

       430        440        450        460        470        480 
EYVPEGVEAA TPYKGSLASE LHQLVGGIQS GMGYVGAESI PAFKADAEFV RVSAAGQTEG 

       490 
HPHDVMITDE APNYSPQGE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004437 Genomic DNA. Translation: AAG19418.1. Different initiation.
PIRF84256.
RefSeqNP_279938.1. NC_002607.1.

3D structure databases

ProteinModelPortalQ9HQU4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING64091.VNG1001G.

Proteomic databases

PaxDbQ9HQU4.
PRIDEQ9HQU4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG19418; AAG19418; VNG_1001G.
GeneID1447720.
KEGGhal:VNG1001G.

Phylogenomic databases

eggNOGCOG0517.
KOK00088.
OMANAIRGYT.
PhylomeDBQ9HQU4.

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_HALSA
AccessionPrimary (citable) accession number: Q9HQU4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: April 3, 2013
Last modified: May 14, 2014
This is version 84 of the entry and version 2 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