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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229)
Status
Reviewed-Annotation score: Annotation score: 3 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 sitei250NADUniRule annotation1
Metal bindingi302Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi304Potassium; via carbonyl oxygenUniRule annotation1
Binding sitei305IMPUniRule annotation1
Active sitei307Thioimidate intermediateUniRule annotation1
Metal bindingi307Potassium; via carbonyl oxygenUniRule annotation1
Active sitei403Proton acceptorUniRule annotation1
Binding sitei417IMPUniRule annotation1
Metal bindingi471Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi472Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi473Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi300 – 302NADUniRule 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:SSP2323
OrganismiStaphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229)
Taxonomic identifieri342451 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000006371 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002873631 – 488Inosine-5'-monophosphate dehydrogenaseAdd BLAST488

Proteomic databases

PRIDEiQ49UU8.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi342451.SSP2323.

Structurei

3D structure databases

ProteinModelPortaliQ49UU8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini95 – 153CBS 1UniRule annotationAdd BLAST59
Domaini157 – 216CBS 2UniRule annotationAdd BLAST60

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni340 – 342IMP bindingUniRule annotation3
Regioni363 – 364IMP bindingUniRule annotation2
Regioni387 – 391IMP 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.
HOGENOMiHOG000165754.
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.

Q49UU8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWENKFEKES LTFDDVLLLP AESDVLPKEV DLSVQLSEGI KLNIPVISAG
60 70 80 90 100
MDTVTESKMA ISMARQGGLG VIHKNMNIED QADEVQKVKR SENGVISNPF
110 120 130 140 150
FLTPEESVFE AEALMGKYRI SGVPIVNNKE DRQFVGIITN RDLRFIEDFS
160 170 180 190 200
IKISDVMTKE QLVTAPVGTT LDEAEKLLQQ HKIEKLPLVK EGRLEGLITI
210 220 230 240 250
KDIEKVLEFP NSAKDEHGRL LVGAAIGIAK DTDIRAQKLV EAGVDALVID
260 270 280 290 300
TAHGHSKGVL EQVKHIKETF PQVTLIAGNV ATAEGTKALY EAGADVVKVG
310 320 330 340 350
IGPGSICTTR VVAGVGVPQI TAVYDCATEA RKHGKAIIAD GGIKFSGDII
360 370 380 390 400
KALAAGGHAV MLGSLLAGTE ESPGATEVFQ GRQYKVYRGM GSLGAMESGS
410 420 430 440 450
NDRYFQEDKA PKKFVPEGIE GRIAYKGSLQ DTIYQLMGGV RSGMGYTGSR
460 470 480
NLEALREEAQ FTRMGPAGLA ESHPHDVQIT KESPNYSF
Length:488
Mass (Da):52,723
Last modified:September 13, 2005 - v1
Checksum:i9463DB596C8EFEDD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008934 Genomic DNA. Translation: BAE19468.1.
RefSeqiWP_002484264.1. NC_007350.1.

Genome annotation databases

EnsemblBacteriaiBAE19468; BAE19468; SSP2323.
GeneIDi3616569.
KEGGissp:SSP2323.
PATRICi19626259. VBIStaSap90642_2312.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008934 Genomic DNA. Translation: BAE19468.1.
RefSeqiWP_002484264.1. NC_007350.1.

3D structure databases

ProteinModelPortaliQ49UU8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi342451.SSP2323.

Proteomic databases

PRIDEiQ49UU8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAE19468; BAE19468; SSP2323.
GeneIDi3616569.
KEGGissp:SSP2323.
PATRICi19626259. VBIStaSap90642_2312.

Phylogenomic databases

eggNOGiENOG4105CP4. Bacteria.
COG0516. LUCA.
COG0517. LUCA.
HOGENOMiHOG000165754.
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_STAS1
AccessioniPrimary (citable) accession number: Q49UU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: September 13, 2005
Last modified: November 2, 2016
This is version 83 of the entry and version 1 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.