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A9A5Y7

- IMDH_NITMS

UniProt

A9A5Y7 - IMDH_NITMS

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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Nitrosopumilus maritimus (strain SCM1)
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

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 sitei244 – 2441NADUniRule annotation
Metal bindingi296 – 2961Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi298 – 2981Potassium; via carbonyl oxygenUniRule annotation
Binding sitei299 – 2991IMPUniRule annotation
Active sitei301 – 3011Thioimidate intermediateUniRule annotation
Metal bindingi301 – 3011Potassium; via carbonyl oxygenUniRule annotation
Binding sitei413 – 4131IMPUniRule annotation
Metal bindingi467 – 4671Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi468 – 4681Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi294 – 2963NADUniRule 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

BioCyciNMAR436308:GI3J-1613-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:Nmar_1569
OrganismiNitrosopumilus maritimus (strain SCM1)
Taxonomic identifieri436308 [NCBI]
Taxonomic lineageiArchaeaThaumarchaeotaNitrosopumilalesNitrosopumilaceaeNitrosopumilus
ProteomesiUP000000792: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 476476Inosine-5'-monophosphate dehydrogenasePRO_0000415694Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi436308.Nmar_1569.

Structurei

3D structure databases

ProteinModelPortaliA9A5Y7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini92 – 15059CBS 1UniRule annotationAdd
BLAST
Domaini151 – 20757CBS 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni334 – 3363IMP bindingUniRule annotation
Regioni357 – 3582IMP bindingUniRule annotation
Regioni381 – 3855IMP 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.
OMAiHGHSKNI.

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.

A9A5Y7 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEFKEGLTFD DVLLVPKYSD ITSRSQTDLT TKLSRNITIN IPFVSANMDT
60 70 80 90 100
VTESSMAVAM ARAGGIGIIH RFLTIQEQAN EVLKVKRSGS VMIENPYSIS
110 120 130 140 150
SDKSIQDALD YAEDKEISGL LVVDSNSKLV GIVTERDLLF AGSNGTIADV
160 170 180 190 200
MTKDVVTAKP GVSLDEAKDI LHKHRIEKLP IVDDSGIIQG LITSKDITNN
210 220 230 240 250
TDYPNASKDK KGRPLVGAAV GVKGDFLERS ESLLNAGADV LVVDIAHGHS
260 270 280 290 300
ENAISTVRNI KKAFPDCELI AGNIATAQGA EDLIKAGVDA VKVGVGSGSI
310 320 330 340 350
CITRVITGSG VPQLTAVMDC AKIGNDHGIP IISDGGTRTS GDATKALAAG
360 370 380 390 400
ASSVMVGSML GGTDESPGTV LTKNGKRFKV YRGMASLAAS IGRKSKETGS
410 420 430 440 450
ISLEDDLNDY VAEGVEAMVP YKGTVTDILK QLAGGVRSGL SYCGAHTIPQ
460 470
MQQNAEFIKM SRAGFAESQP HDVLLM
Length:476
Mass (Da):50,130
Last modified:January 15, 2008 - v1
Checksum:i19BE67B0C7883900
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000866 Genomic DNA. Translation: ABX13465.1.
RefSeqiWP_012215952.1. NC_010085.1.
YP_001582903.1. NC_010085.1.

Genome annotation databases

EnsemblBacteriaiABX13465; ABX13465; Nmar_1569.
GeneIDi5772999.
KEGGinmr:Nmar_1569.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000866 Genomic DNA. Translation: ABX13465.1 .
RefSeqi WP_012215952.1. NC_010085.1.
YP_001582903.1. NC_010085.1.

3D structure databases

ProteinModelPortali A9A5Y7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 436308.Nmar_1569.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABX13465 ; ABX13465 ; Nmar_1569 .
GeneIDi 5772999.
KEGGi nmr:Nmar_1569.

Phylogenomic databases

eggNOGi COG0517.
HOGENOMi HOG000165755.
KOi K00088.
OMAi HGHSKNI.

Enzyme and pathway databases

UniPathwayi UPA00601 ; UER00295 .
BioCyci NMAR436308:GI3J-1613-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: SCM1.

Entry informationi

Entry nameiIMDH_NITMS
AccessioniPrimary (citable) accession number: A9A5Y7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: January 15, 2008
Last modified: October 29, 2014
This is version 46 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, 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