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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Status
Reviewed-Annotation score: 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

Pathway:iXMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes XMP from IMP.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Inosine-5'-monophosphate dehydrogenase (guaB)
This subpathway is part of the pathway XMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes XMP from IMP, the pathway XMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei283 – 2831NADUniRule annotation
Metal bindingi336 – 3361Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi338 – 3381Potassium; via carbonyl oxygenUniRule annotation
Binding sitei339 – 3391IMPUniRule annotation
Active sitei341 – 3411Thioimidate intermediateUniRule annotation
Metal bindingi341 – 3411Potassium; via carbonyl oxygenUniRule annotation
Binding sitei458 – 4581IMPUniRule annotation
Metal bindingi511 – 5111Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi512 – 5121Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi513 – 5131Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi334 – 3363NADUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

GMP biosynthesis, Purine biosynthesis

Keywords - Ligandi

Metal-binding, NAD, Potassium

Enzyme and pathway databases

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:Mb3445c
OrganismiMycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Taxonomic identifieri233413 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
ProteomesiUP000001419 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 529529Inosine-5'-monophosphate dehydrogenasePRO_0000093700Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP65168.
SMRiP65168. Positions 44-526.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini129 – 18557CBS 1UniRule annotationAdd
BLAST
Domaini189 – 24658CBS 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni374 – 3763IMP bindingUniRule annotation
Regioni397 – 3982IMP bindingUniRule annotation
Regioni421 – 4255IMP 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.
OMAiSSMGYCG.
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.

P65168-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRGMSGLED SSDLVVSPYV RMGGLTTDPV PTGGDDPHKV AMLGLTFDDV
60 70 80 90 100
LLLPAASDVV PATADTSSQL TKKIRLKVPL VSSAMDTVTE SRMAIAMARA
110 120 130 140 150
GGMGVLHRNL PVAEQAGQVE MVKRSEAGMV TDPVTCRPDN TLAQVDALCA
160 170 180 190 200
RFRISGLPVV DDDGALVGII TNRDMRFEVD QSKQVAEVMT KAPLITAQEG
210 220 230 240 250
VSASAALGLL RRNKIEKLPV VDGRGRLTGL ITVKDFVKTE QHPLATKDSD
260 270 280 290 300
GRLLVGAAVG VGGDAWVRAM MLVDAGVDVL VVDTAHAHNR LVLDMVGKLK
310 320 330 340 350
SEVGDRVEVV GGNVATRSAA AALVDAGADA VKVGVGPGSI CTTRVVAGVG
360 370 380 390 400
APQITAILEA VAACRPAGVP VIADGGLQYS GDIAKALAAG ASTAMLGSLL
410 420 430 440 450
AGTAEAPGEL IFVNGKQYKS YRGMGSLGAM RGRGGATSYS KDRYFADDAL
460 470 480 490 500
SEDKLVPEGI EGRVPFRGPL SSVIHQLTGG LRAAMGYTGS PTIEVLQQAQ
510 520
FVRITPAGLK ESHPHDVAMT VEAPNYYAR
Length:529
Mass (Da):54,867
Last modified:October 11, 2004 - v1
Checksum:i689A7C7C53993C0A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX248333 Genomic DNA. Translation: CDO44716.1.
RefSeqiNP_857085.1. NC_002945.3.
WP_003900682.1. NC_002945.3.

Genome annotation databases

EnsemblBacteriaiCDO44716; CDO44716; Mb3445c.
GeneIDi1091016.
KEGGimbo:Mb3445c.
PATRICi18009304. VBIMycBov88188_3780.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX248333 Genomic DNA. Translation: CDO44716.1.
RefSeqiNP_857085.1. NC_002945.3.
WP_003900682.1. NC_002945.3.

3D structure databases

ProteinModelPortaliP65168.
SMRiP65168. Positions 44-526.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCDO44716; CDO44716; Mb3445c.
GeneIDi1091016.
KEGGimbo:Mb3445c.
PATRICi18009304. VBIMycBov88188_3780.

Phylogenomic databases

eggNOGiCOG0517.
HOGENOMiHOG000165755.
KOiK00088.
OMAiSSMGYCG.
OrthoDBiEOG6GTZPV.

Enzyme and pathway databases

UniPathwayiUPA00601; UER00295.

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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-935 / AF2122/97.

Entry informationi

Entry nameiIMDH_MYCBO
AccessioniPrimary (citable) accession number: P65168
Secondary accession number(s): Q50715, X2BPI0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: July 22, 2015
This is version 82 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.