Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Staphylococcus aureus (strain N315)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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

Pathway: 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei250 – 2501NADUniRule annotation
Metal bindingi302 – 3021Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi304 – 3041Potassium; via carbonyl oxygenUniRule annotation
Binding sitei305 – 3051IMPUniRule annotation
Active sitei307 – 3071Thioimidate intermediateUniRule annotation
Metal bindingi307 – 3071Potassium; via carbonyl oxygenUniRule annotation
Binding sitei417 – 4171IMPUniRule annotation
Metal bindingi471 – 4711Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi472 – 4721Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi473 – 4731Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi300 – 3023NADUniRule annotation

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

BioCyciSAUR158879:GJCB-387-MONOMER.
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:SA0375
OrganismiStaphylococcus aureus (strain N315)
Taxonomic identifieri158879 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 488488Inosine-5'-monophosphate dehydrogenasePRO_0000093708Add
BLAST

Proteomic databases

PRIDEiP99106.

2D gel databases

SWISS-2DPAGEP99106.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP99106.
SMRiP99106. Positions 1-487.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini95 – 15359CBS 1UniRule annotationAdd
BLAST
Domaini157 – 21660CBS 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni340 – 3423IMP bindingUniRule annotation
Regioni363 – 3642IMP bindingUniRule annotation
Regioni387 – 3915IMP bindingUniRule annotation

Sequence similaritiesi

Belongs to the IMPDH/GMPR family.UniRule annotation
Contains 2 CBS domains.UniRule annotation

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiCOG0517.
HOGENOMiHOG000165754.
KOiK00088.
OMAiSSMGYCG.
OrthoDBiEOG6GTZPV.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH.
InterProiIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
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.

P99106-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWESKFAKES LTFDDVLLIP AQSDILPKDV DLSVQLSDKV KLNIPVISAG
60 70 80 90 100
MDTVTESKMA IAMARQGGLG VIHKNMGVEE QADEVQKVKR SENGVISNPF
110 120 130 140 150
FLTPEESVYE AEALMGKYRI SGVPIVDNKE DRNLVGILTN RDLRFIEDFS
160 170 180 190 200
IKIVDVMTQE NLITAPVNTT LEEAEKILQK HKIEKLPLVK DGRLEGLITI
210 220 230 240 250
KDIEKVIEFP NAAKDEHGRL LVAAAIGISK DTDIRAQKLV EAGVDVLVID
260 270 280 290 300
TAHGHSKGVI DQVKHIKKTY PEITLVAGNV ATAEATKDLF EAGADIVKVG
310 320 330 340 350
IGPGSICTTR VVAGVGVPQI TAIYDCATEA RKHGKAIIAD GGIKFSGDII
360 370 380 390 400
KALAAGGHAV MLGSLLAGTE ESPGATEIFQ GRQYKVYRGM GSLGAMEKGS
410 420 430 440 450
NDRYFQEDKA PKKFVPEGIE GRTAYKGALQ DTIYQLMGGV RAGMGYTGSH
460 470 480
DLRELREEAQ FTRMGPAGLA ESHPHNIQIT KESPNYSF
Length:488
Mass (Da):52,851
Last modified:October 11, 2004 - v1
Checksum:iC4E945D25D41491D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA. Translation: BAB41602.1.
PIRiG89805.
RefSeqiNP_373624.1. NC_002745.2.
WP_000264071.1. NC_002745.2.

Genome annotation databases

EnsemblBacteriaiBAB41602; BAB41602; BAB41602.
GeneIDi23197582.
KEGGisau:SA0375.
PATRICi19572814. VBIStaAur116463_0396.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA. Translation: BAB41602.1.
PIRiG89805.
RefSeqiNP_373624.1. NC_002745.2.
WP_000264071.1. NC_002745.2.

3D structure databases

ProteinModelPortaliP99106.
SMRiP99106. Positions 1-487.
ModBaseiSearch...
MobiDBiSearch...

2D gel databases

SWISS-2DPAGEP99106.

Proteomic databases

PRIDEiP99106.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB41602; BAB41602; BAB41602.
GeneIDi23197582.
KEGGisau:SA0375.
PATRICi19572814. VBIStaAur116463_0396.

Phylogenomic databases

eggNOGiCOG0517.
HOGENOMiHOG000165754.
KOiK00088.
OMAiSSMGYCG.
OrthoDBiEOG6GTZPV.

Enzyme and pathway databases

UniPathwayiUPA00601; UER00295.
BioCyciSAUR158879:GJCB-387-MONOMER.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH.
InterProiIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: N315.
  2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: N315.
  3. "Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
    Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.
    Submitted (OCT-2007) to UniProtKB
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: N315.

Entry informationi

Entry nameiIMDH_STAAN
AccessioniPrimary (citable) accession number: P99106
Secondary accession number(s): Q99WI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: June 24, 2015
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.