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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium)
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 sitei260NADUniRule annotation1
Metal bindingi310Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi312Potassium; via carbonyl oxygenUniRule annotation1
Binding sitei313IMPUniRule annotation1
Active sitei315Thioimidate intermediateUniRule annotation1
Metal bindingi315Potassium; via carbonyl oxygenUniRule annotation1
Active sitei411Proton acceptorUniRule annotation1
Binding sitei425IMPUniRule annotation1
Metal bindingi479Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi480Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi481Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi308 – 310NADUniRule 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:VNG_1001G
OrganismiHalobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium)
Taxonomic identifieri64091 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHalobacterium
Proteomesi
  • UP000000554 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004156921 – 499Inosine-5'-monophosphate dehydrogenaseAdd BLAST499

Proteomic databases

PaxDbiQ9HQU4.
PRIDEiQ9HQU4.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi64091.VNG1001G.

Structurei

3D structure databases

ProteinModelPortaliQ9HQU4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini106 – 165CBS 1UniRule annotationAdd BLAST60
Domaini169 – 225CBS 2UniRule annotationAdd BLAST57

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni348 – 350IMP bindingUniRule annotation3
Regioni371 – 372IMP bindingUniRule annotation2
Regioni395 – 399IMP 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

eggNOGiarCOG00612. Archaea.
ENOG4102TCX. Archaea.
COG0516. LUCA.
COG0517. LUCA.
InParanoidiQ9HQU4.
KOiK00088.
PhylomeDBiQ9HQU4.

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.

Q9HQU4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANDSSTDGR FSEKLRVPEA LTFDDVLLRP AESRVEPDDA DVATRVSTNV
60 70 80 90 100
ELEVPVLSAA MDTVTESRLA IAMAREGGLG VLHQNMDTDR VVAEVERVKR
110 120 130 140 150
ADELVIDREN VVTAAPEQTV EAVDEMMDRS DVSGAPVVDD DDTVRGIISA
160 170 180 190 200
TDIRPYLEVG ESDAVREAMT DEVITAPEDI TARDALELMY EHKIERVPIV
210 220 230 240 250
NDEQHLVGLV TMQGILERRE HGSAARDQNG RLRVGVAVGP FDTERATAVD
260 270 280 290 300
EAGADVLFID CAHAHNLNVI DSAREIKASV DADVVVGNVG TREAAEAVVD
310 320 330 340 350
FADGIKVGIG PGSICTTRVV TGSGMPQITA VSQVADVAAP AGVPVIADGG
360 370 380 390 400
IRYSGDAAKA IAAGADAVML GSYFAGTDEA PGRVITMNGK KYKQYRGMGS
410 420 430 440 450
VGAMQSGGSD RYLKDDDEDE EYVPEGVEAA TPYKGSLASE LHQLVGGIQS
460 470 480 490
GMGYVGAESI PAFKADAEFV RVSAAGQTEG HPHDVMITDE APNYSPQGE
Length:499
Mass (Da):52,767
Last modified:April 3, 2013 - v2
Checksum:i3A6C3B23A42B9D39
GO

Sequence cautioni

The sequence AAG19418 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004437 Genomic DNA. Translation: AAG19418.1. Different initiation.
PIRiF84256.
RefSeqiWP_012289261.1. NC_002607.1.

Genome annotation databases

EnsemblBacteriaiAAG19418; AAG19418; VNG_1001G.
GeneIDi5952782.
KEGGihal:VNG_1001G.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004437 Genomic DNA. Translation: AAG19418.1. Different initiation.
PIRiF84256.
RefSeqiWP_012289261.1. NC_002607.1.

3D structure databases

ProteinModelPortaliQ9HQU4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi64091.VNG1001G.

Proteomic databases

PaxDbiQ9HQU4.
PRIDEiQ9HQU4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG19418; AAG19418; VNG_1001G.
GeneIDi5952782.
KEGGihal:VNG_1001G.

Phylogenomic databases

eggNOGiarCOG00612. Archaea.
ENOG4102TCX. Archaea.
COG0516. LUCA.
COG0517. LUCA.
InParanoidiQ9HQU4.
KOiK00088.
PhylomeDBiQ9HQU4.

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_HALSA
AccessioniPrimary (citable) accession number: Q9HQU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: April 3, 2013
Last modified: November 2, 2016
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference 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.