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P0C0H7

- IMDH_STRP1

UniProt

P0C0H7 - IMDH_STRP1

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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Streptococcus pyogenes serotype M1
Status
Reviewed - Annotation score: 4 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 sitei253 – 2531NADUniRule annotation
Metal bindingi305 – 3051Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi307 – 3071Potassium; via carbonyl oxygenUniRule annotation
Binding sitei308 – 3081IMPUniRule annotation
Active sitei310 – 3101Thioimidate intermediateUniRule annotation
Metal bindingi310 – 3101Potassium; via carbonyl oxygenUniRule annotation
Binding sitei421 – 4211IMPUniRule annotation
Metal bindingi475 – 4751Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi476 – 4761Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi477 – 4771Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi303 – 3053NADUniRule 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

BioCyciSPYO160490:GJ81-1800-MONOMER.
SPYO293653:GHFC-1938-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:SPy_2206, M5005_Spy1857
OrganismiStreptococcus pyogenes serotype M1
Taxonomic identifieri301447 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
ProteomesiUP000000750: Chromosome, UP000002702: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 493492Inosine-5'-monophosphate dehydrogenasePRO_0000093715Add
BLAST

Proteomic databases

PaxDbiP0C0H7.
PRIDEiP0C0H7.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi160490.SPy_2206.

Structurei

3D structure databases

ProteinModelPortaliP0C0H7.
SMRiP0C0H7. Positions 2-491.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini97 – 15559CBS 1UniRule annotationAdd
BLAST
Domaini159 – 21961CBS 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni343 – 3453IMP bindingUniRule annotation
Regioni366 – 3672IMP bindingUniRule annotation
Regioni390 – 3945IMP 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.
HOGENOMiHOG000165755.
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]
PANTHERiPTHR11911:SF6. PTHR11911:SF6. 1 hit.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0C0H7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSNWDTKFLK KGYTFDDVLL IPAESHVLPN EVDLKTKLAD NLTLNIPIIT
60 70 80 90 100
AAMDTVTGSK MAIAIARAGG LGVIHKNMSI TEQAEEVRKV KRSENGVIID
110 120 130 140 150
PFFLTPEHKV SEAEELMQRY RISGVPIVET LANRKLVGII TNRDMRFISD
160 170 180 190 200
YNAPISEHMT SEHLVTAAVG TDLETAERIL HEHRIEKLPL VDNSGRLSGL
210 220 230 240 250
ITIKDIEKVI EFPHAAKDEF GRLLVAAAVG VTSDTFERAE ALFEAGADAI
260 270 280 290 300
VIDTAHGHSA GVLRKIAEIR AHFPNRTLIA GNIATAEGAR ALYDAGVDVV
310 320 330 340 350
KVGIGPGSIC TTRVVAGVGV PQVTAIYDAA AVAREYGKTI IADGGIKYSG
360 370 380 390 400
DIVKALAAGG NAVMLGSMFA GTDEAPGETE IYQGRKFKTY RGMGSIAAMK
410 420 430 440 450
KGSSDRYFQG SVNEANKLVP EGIEGRVAYK GAASDIVFQM LGGIRSGMGY
460 470 480 490
VGAGDIQELH ENAQFVEMSG AGLIESHPHD VQITNEAPNY SVH
Length:493
Mass (Da):52,807
Last modified:January 23, 2007 - v2
Checksum:i9C317AD598CB5740
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004092 Genomic DNA. Translation: AAK34834.1.
CP000017 Genomic DNA. Translation: AAZ52475.1.
RefSeqiNP_270113.1. NC_002737.1.
YP_283220.1. NC_007297.1.

Genome annotation databases

EnsemblBacteriaiAAK34834; AAK34834; SPy_2206.
AAZ52475; AAZ52475; M5005_Spy1857.
GeneIDi3571029.
901896.
KEGGispy:SPy_2206.
spz:M5005_Spy_1857.
PATRICi19717735. VBIStrPyo79812_1911.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004092 Genomic DNA. Translation: AAK34834.1 .
CP000017 Genomic DNA. Translation: AAZ52475.1 .
RefSeqi NP_270113.1. NC_002737.1.
YP_283220.1. NC_007297.1.

3D structure databases

ProteinModelPortali P0C0H7.
SMRi P0C0H7. Positions 2-491.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 160490.SPy_2206.

Chemistry

BindingDBi P0C0H7.

Proteomic databases

PaxDbi P0C0H7.
PRIDEi P0C0H7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK34834 ; AAK34834 ; SPy_2206 .
AAZ52475 ; AAZ52475 ; M5005_Spy1857 .
GeneIDi 3571029.
901896.
KEGGi spy:SPy_2206.
spz:M5005_Spy_1857.
PATRICi 19717735. VBIStrPyo79812_1911.

Phylogenomic databases

eggNOGi COG0517.
HOGENOMi HOG000165755.
KOi K00088.
OMAi HAAKDEH.
OrthoDBi EOG6GTZPV.

Enzyme and pathway databases

UniPathwayi UPA00601 ; UER00295 .
BioCyci SPYO160490:GJ81-1800-MONOMER.
SPYO293653:GHFC-1938-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 ]
PANTHERi PTHR11911:SF6. PTHR11911:SF6. 1 hit.
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: ATCC 700294 / SF370 / Serotype M1.
  2. "Evolutionary origin and emergence of a highly successful clone of serotype M1 group A Streptococcus involved multiple horizontal gene transfer events."
    Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K., Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P., Musser J.M.
    J. Infect. Dis. 192:771-782(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-947 / MGAS5005 / Serotype M1.

Entry informationi

Entry nameiIMDH_STRP1
AccessioniPrimary (citable) accession number: P0C0H7
Secondary accession number(s): P50099, P68838, Q48W00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 72 of the entry and version 2 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

External Data

Dasty 3