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UniProtKB - P65168 (IMDH_MYCBO)

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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

Pathwayi: XMP 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)DescriptionActionsGraphical viewLength
Binding sitei283NADUniRule annotation1
Metal bindingi336Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi338Potassium; via carbonyl oxygenUniRule annotation1
Binding sitei339IMPUniRule annotation1
Active sitei341Thioimidate intermediateUniRule annotation1
Metal bindingi341Potassium; via carbonyl oxygenUniRule annotation1
Active sitei443Proton acceptorUniRule annotation1
Binding sitei458IMPUniRule annotation1
Metal bindingi511Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi512Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi513Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi334 – 336NADUniRule annotation3

GO - Molecular functioni

Complete GO annotation...

GO - Biological processi

Complete GO annotation...

Keywordsi

Molecular functionOxidoreductase
Biological processGMP biosynthesis, Purine biosynthesis
LigandMetal-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:BQ2027_MB3445C
OrganismiMycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Taxonomic identifieri233413 [NCBI]
Taxonomic lineageiBacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex ›
Proteomesi
  • UP000001419 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000937001 – 529Inosine-5'-monophosphate dehydrogenaseAdd BLAST529

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP65168.
SMRiP65168.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini129 – 185CBS 1UniRule annotationAdd BLAST57
Domaini189 – 246CBS 2UniRule annotationAdd BLAST58

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni374 – 376IMP bindingUniRule annotation3
Regioni397 – 398IMP bindingUniRule annotation2
Regioni421 – 425IMP bindingUniRule annotation5

Sequence similaritiesi

Belongs to the IMPDH/GMPR family.UniRule annotation

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

HOGENOMiHOG000165755.
KOiK00088.
OMAiGIGIVHK.

Family and domain databases

CDDicd00381. IMPDH. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH. 1 hit.
InterProiView protein in InterPro
IPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
PfamiView protein in Pfam
PF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
PIRSFiPIRSF000130. IMPDH. 1 hit.
SMARTiView protein in SMART
SM00116. CBS. 2 hits.
TIGRFAMsiTIGR01302. IMP_dehydrog. 1 hit.
PROSITEiView protein in PROSITE
PS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.

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
LT708304 Genomic DNA. Translation: SIU02073.1.
RefSeqiNP_857085.1. NC_002945.3.
WP_003900682.1. NC_002945.3.

Genome annotation databases

EnsemblBacteriaiCDO44716; CDO44716; Mb3445c.
GeneIDi1091016.
KEGGimbo:Mb3445c.
PATRICifig|233413.5.peg.3780.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
LT708304 Genomic DNA. Translation: SIU02073.1.
RefSeqiNP_857085.1. NC_002945.3.
WP_003900682.1. NC_002945.3.

3D structure databases

ProteinModelPortaliP65168.
SMRiP65168.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCDO44716; CDO44716; Mb3445c.
GeneIDi1091016.
KEGGimbo:Mb3445c.
PATRICifig|233413.5.peg.3780.

Phylogenomic databases

HOGENOMiHOG000165755.
KOiK00088.
OMAiGIGIVHK.

Enzyme and pathway databases

UniPathwayiUPA00601; UER00295.

Family and domain databases

CDDicd00381. IMPDH. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH. 1 hit.
InterProiView protein in InterPro
IPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
PfamiView protein in Pfam
PF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
PIRSFiPIRSF000130. IMPDH. 1 hit.
SMARTiView protein in SMART
SM00116. CBS. 2 hits.
TIGRFAMsiTIGR01302. IMP_dehydrog. 1 hit.
PROSITEiView protein in PROSITE
PS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiIMDH_MYCBO
AccessioniPrimary (citable) accession number: P65168
Secondary accession number(s): A0A1R3Y452, Q50715, X2BPI0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: June 7, 2017
This is version 93 of the entry and version 1 of the sequence. See 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

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 one 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.