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Q8NY70

- IMDH_STAAW

UniProt

Q8NY70 - IMDH_STAAW

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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Staphylococcus aureus (strain MW2)
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.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

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

BioCyciSAUR196620:GJ9Z-368-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:MW0366
OrganismiStaphylococcus aureus (strain MW2)
Taxonomic identifieri196620 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000418: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 488488Inosine-5'-monophosphate dehydrogenasePRO_0000093711Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi196620.MW0366.

Structurei

3D structure databases

ProteinModelPortaliQ8NY70.
SMRiQ8NY70. Positions 2-487.
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.
OMAiHAAKDEH.
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.

Q8NY70-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MWESKFAKES LTFDDVLLIP AQSDILPKDV DLSVQLSDKA 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):52,823
Last modified:October 1, 2002 - v1
Checksum:i78138D81A88615E7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000033 Genomic DNA. Translation: BAB94231.1.
RefSeqiNP_645183.1. NC_003923.1.
WP_000264068.1. NC_003923.1.

Genome annotation databases

EnsemblBacteriaiBAB94231; BAB94231; BAB94231.
GeneIDi1002466.
KEGGisam:MW0366.
PATRICi19567214. VBIStaAur44266_0389.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000033 Genomic DNA. Translation: BAB94231.1 .
RefSeqi NP_645183.1. NC_003923.1.
WP_000264068.1. NC_003923.1.

3D structure databases

ProteinModelPortali Q8NY70.
SMRi Q8NY70. Positions 2-487.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 196620.MW0366.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB94231 ; BAB94231 ; BAB94231 .
GeneIDi 1002466.
KEGGi sam:MW0366.
PATRICi 19567214. VBIStaAur44266_0389.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00601 ; UER00295 .
BioCyci SAUR196620:GJ9Z-368-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MW2.

Entry informationi

Entry nameiIMDH_STAAW
AccessioniPrimary (citable) accession number: Q8NY70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: October 1, 2002
Last modified: November 26, 2014
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

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