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P99106

- IMDH_STAAN

UniProt

P99106 - IMDH_STAAN

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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Staphylococcus aureus (strain N315)
Status
Reviewed - 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

Potassium.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

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

  1. adenyl nucleotide binding Source: InterPro
  2. IMP dehydrogenase activity Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. GMP biosynthetic process Source: UniProtKB-HAMAP
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
ProteomesiUP000000751: Chromosome

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

Protein-protein interaction databases

STRINGi158879.SA0375.

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.
OMAiHGHSKNI.
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 [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:
EMBL
GenBank
DDBJ
Links Updated
BA000018 Genomic DNA. Translation: BAB41602.1.
PIRiG89805.
RefSeqiNP_373624.1. NC_002745.2.

Genome annotation databases

EnsemblBacteriaiBAB41602; BAB41602; BAB41602.
GeneIDi1123157.
KEGGisau:SA0375.
PATRICi19572814. VBIStaAur116463_0396.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000018 Genomic DNA. Translation: BAB41602.1 .
PIRi G89805.
RefSeqi NP_373624.1. NC_002745.2.

3D structure databases

ProteinModelPortali P99106.
SMRi P99106. Positions 1-487.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 158879.SA0375.

2D gel databases

SWISS-2DPAGE P99106.

Proteomic databases

PRIDEi P99106.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB41602 ; BAB41602 ; BAB41602 .
GeneIDi 1123157.
KEGGi sau:SA0375.
PATRICi 19572814. VBIStaAur116463_0396.

Phylogenomic databases

eggNOGi COG0517.
HOGENOMi HOG000165754.
KOi K00088.
OMAi HGHSKNI.
OrthoDBi EOG6GTZPV.

Enzyme and pathway databases

UniPathwayi UPA00601 ; UER00295 .
BioCyci SAUR158879:GJCB-387-MONOMER.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_01964. IMPDH.
InterProi IPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view ]
Pfami PF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000130. IMPDH. 1 hit.
SMARTi SM00116. CBS. 2 hits.
[Graphical view ]
TIGRFAMsi TIGR01302. IMP_dehydrog. 1 hit.
PROSITEi PS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 1, 2014
This is version 81 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

Documents

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

External Data

Dasty 3