SubmitCancel

Skip Header

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

Q4L385

- IMDH_STAHJ

UniProt

Q4L385 - IMDH_STAHJ

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Inosine-5'-monophosphate dehydrogenase
Gene
guaB, SH2583
Organism
Staphylococcus haemolyticus (strain JCSC1435)
Status
Reviewed - 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 By similarity.UniRule annotation

Catalytic activityi

Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH.UniRule annotation

Cofactori

Potassium By similarity.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 By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei250 – 2501NAD By similarity
Metal bindingi302 – 3021Potassium; via carbonyl oxygen By similarity
Metal bindingi304 – 3041Potassium; via carbonyl oxygen By similarity
Binding sitei305 – 3051IMP By similarity
Active sitei307 – 3071Thioimidate intermediate By similarity
Metal bindingi307 – 3071Potassium; via carbonyl oxygen By similarity
Binding sitei417 – 4171IMP By similarity
Metal bindingi471 – 4711Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi472 – 4721Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi473 – 4731Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi300 – 3023NAD By similarity

GO - Molecular functioni

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

BioCyciSHAE279808:GJX7-2658-MONOMER.
UniPathwayiUPA00601; UER00295.

Names & Taxonomyi

Protein namesi
Recommended name:
Inosine-5'-monophosphate dehydrogenase (EC:1.1.1.205)
Short name:
IMP dehydrogenase
Short name:
IMPD
Short name:
IMPDH
Gene namesi
Name:guaB
Ordered Locus Names:SH2583
OrganismiStaphylococcus haemolyticus (strain JCSC1435)
Taxonomic identifieri279808 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000543: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 488488Inosine-5'-monophosphate dehydrogenaseUniRule annotation
PRO_0000287362Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi279808.SH2583.

Structurei

3D structure databases

ProteinModelPortaliQ4L385.
SMRiQ4L385. Positions 2-487.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini95 – 15359CBS 1
Add
BLAST
Domaini157 – 21357CBS 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni340 – 3423IMP binding By similarity
Regioni363 – 3642IMP binding By similarity
Regioni387 – 3915IMP binding By similarity

Sequence similaritiesi

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

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiCOG0517.
HOGENOMiHOG000165752.
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.

Q4L385-1 [UniParc]FASTAAdd to Basket

« Hide

MWENKFAKES LTFDDVLLIP AASDVLPNDA DLSVELSERI KLNIPVISAG    50
MDTVTESKMA IAMARQGGLG VIHKNMGIEE QAEEVQKVKR SENGVITNPF 100
YLTPDESVYE AEALMGKYRI SGVPIVSDKE SRELVGILTN RDLRFIEDFS 150
IKISDVMTKE NLITAPVGTT LDEAETILQE HKIEKLPLVE NGRLEGLITI 200
KDIEKVLEFP HAAKDAHGRL LAAAAIGTSK DTEIRAQKLV EAGVDALIID 250
TAHGHSSGVI QEVKKMKEKY PEITIVAGNV ATAEATRALF EAGADVVKVG 300
IGPGSICTTR VVAGVGVPQI TAIYDCATEA RKFGKAIIAD GGIKFSGDII 350
KALAAGGHAV MLGSLLAGTE ESPGATEVFQ GRQYKVYRGM GSLGAMEKGS 400
NDRYFQEDKT PRKFVPEGIE GRTAYKGPLQ DTIYQLMGGV RAGMGYTGSP 450
DLKTLRDEAQ FTRMGPAGLA ESHPHNVQIT KESPNYSF 488
Length:488
Mass (Da):52,577
Last modified:August 2, 2005 - v1
Checksum:i2B088725A4CA337B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP006716 Genomic DNA. Translation: BAE05892.1.
RefSeqiYP_254498.1. NC_007168.1.

Genome annotation databases

EnsemblBacteriaiBAE05892; BAE05892; SH2583.
GeneIDi3482174.
KEGGisha:SH2583.
PATRICi19621259. VBIStaHae67511_2532.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP006716 Genomic DNA. Translation: BAE05892.1 .
RefSeqi YP_254498.1. NC_007168.1.

3D structure databases

ProteinModelPortali Q4L385.
SMRi Q4L385. Positions 2-487.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 279808.SH2583.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAE05892 ; BAE05892 ; SH2583 .
GeneIDi 3482174.
KEGGi sha:SH2583.
PATRICi 19621259. VBIStaHae67511_2532.

Phylogenomic databases

eggNOGi COG0517.
HOGENOMi HOG000165752.
KOi K00088.
OMAi HGHSKNI.
OrthoDBi EOG6GTZPV.

Enzyme and pathway databases

UniPathwayi UPA00601 ; UER00295 .
BioCyci SHAE279808:GJX7-2658-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

  1. "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species."
    Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.
    J. Bacteriol. 187:7292-7308(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JCSC1435.

Entry informationi

Entry nameiIMDH_STAHJ
AccessioniPrimary (citable) accession number: Q4L385
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: August 2, 2005
Last modified: June 11, 2014
This is version 70 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

Similar proteinsi