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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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 sitei251NADUniRule annotation1
Metal bindingi303Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi305Potassium; via carbonyl oxygenUniRule annotation1
Binding sitei306IMPUniRule annotation1
Active sitei308Thioimidate intermediateUniRule annotation1
Metal bindingi308Potassium; via carbonyl oxygenUniRule annotation1
Active sitei404Proton acceptorUniRule annotation1
Binding sitei416IMPUniRule annotation1
Metal bindingi470Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi471Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi472Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi301 – 303NADUniRule annotation3

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

BioCyciBSUB:BSU00090-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
Alternative name(s):
Superoxide-inducible protein 12
Short name:
SOI12
Gene namesi
Name:guaBUniRule annotation
Synonyms:gnaB
Ordered Locus Names:BSU00090
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000936911 – 488Inosine-5'-monophosphate dehydrogenaseAdd BLAST488

Proteomic databases

PaxDbiP21879.
PRIDEiP21879.

Expressioni

Inductioni

By superoxide.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

IntActiP21879. 1 interactor.
MINTiMINT-8365336.
STRINGi224308.Bsubs1_010100000045.

Structurei

3D structure databases

ProteinModelPortaliP21879.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini95 – 153CBS 1UniRule annotationAdd BLAST59
Domaini157 – 214CBS 2UniRule annotationAdd BLAST58

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni341 – 343IMP bindingUniRule annotation3
Regioni364 – 365IMP bindingUniRule annotation2
Regioni388 – 392IMP bindingUniRule annotation5

Sequence similaritiesi

Belongs to the IMPDH/GMPR family.UniRule annotation
Contains 2 CBS domains.UniRule annotation

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiENOG4105CP4. Bacteria.
COG0516. LUCA.
COG0517. LUCA.
HOGENOMiHOG000165754.
InParanoidiP21879.
KOiK00088.
OMAiSSMGYCG.
PhylomeDBiP21879.

Family and domain databases

CDDicd00381. IMPDH. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH. 1 hit.
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. 2 hits.
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.

P21879-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWESKFSKEG LTFDDVLLVP AKSEVLPRDV DLSVELTKTL KLNIPVISAG
60 70 80 90 100
MDTVTESAMA IAMARQGGLG IIHKNMSIEQ QAEQVDKVKR SERGVITNPF
110 120 130 140 150
FLTPDHQVFD AEHLMGKYRI SGVPIVNNEE DQKLVGIITN RDLRFISDYS
160 170 180 190 200
MKISDVMTKE ELVTASVGTT LDEAEKILQK HKIEKLPLVD DQNKLKGLIT
210 220 230 240 250
IKDIEKVIEF PNSSKDIHGR LIVGAAVGVT GDTMTRVKKL VEANVDVIVI
260 270 280 290 300
DTAHGHSQGV LNTVTKIRET YPELNIIAGN VATAEATRAL IEAGADVVKV
310 320 330 340 350
GIGPGSICTT RVVAGVGVPQ ITAIYDCATE ARKHGKTIIA DGGIKFSGDI
360 370 380 390 400
TKALAAGGHA VMLGSLLAGT SESPGETEIY QGRRFKVYRG MGSVAAMEKG
410 420 430 440 450
SKDRYFQEEN KKFVPEGIEG RTPYKGPVEE TVYQLVGGLR SGMGYCGSKD
460 470 480
LRALREEAQF IRMTGAGLRE SHPHDVQITK ESPNYTIS
Length:488
Mass (Da):52,991
Last modified:August 29, 2003 - v2
Checksum:i34939E2758EA48B6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti28R → H in CAA39204 (PubMed:1979163).Curated1
Sequence conflicti480 – 488KESPNYTIS → VHRNKALPGLFGSHQKKTGF VYDECCQSGFFSSD in CAA39204 (PubMed:1979163).Curated9

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55669 Genomic DNA. Translation: CAA39204.1.
D26185 Genomic DNA. Translation: BAA05245.1.
AL009126 Genomic DNA. Translation: CAB11785.1.
PIRiS66039. DEBSMP.
RefSeqiNP_387890.1. NC_000964.3.
WP_003226803.1. NZ_JNCM01000024.1.

Genome annotation databases

EnsemblBacteriaiCAB11785; CAB11785; BSU00090.
GeneIDi938032.
KEGGibsu:BSU00090.
PATRICi18971477. VBIBacSub10457_0010.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55669 Genomic DNA. Translation: CAA39204.1.
D26185 Genomic DNA. Translation: BAA05245.1.
AL009126 Genomic DNA. Translation: CAB11785.1.
PIRiS66039. DEBSMP.
RefSeqiNP_387890.1. NC_000964.3.
WP_003226803.1. NZ_JNCM01000024.1.

3D structure databases

ProteinModelPortaliP21879.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP21879. 1 interactor.
MINTiMINT-8365336.
STRINGi224308.Bsubs1_010100000045.

Proteomic databases

PaxDbiP21879.
PRIDEiP21879.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB11785; CAB11785; BSU00090.
GeneIDi938032.
KEGGibsu:BSU00090.
PATRICi18971477. VBIBacSub10457_0010.

Phylogenomic databases

eggNOGiENOG4105CP4. Bacteria.
COG0516. LUCA.
COG0517. LUCA.
HOGENOMiHOG000165754.
InParanoidiP21879.
KOiK00088.
OMAiSSMGYCG.
PhylomeDBiP21879.

Enzyme and pathway databases

UniPathwayiUPA00601; UER00295.
BioCyciBSUB:BSU00090-MONOMER.

Family and domain databases

CDDicd00381. IMPDH. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH. 1 hit.
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. 2 hits.
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...

Entry informationi

Entry nameiIMDH_BACSU
AccessioniPrimary (citable) accession number: P21879
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: August 29, 2003
Last modified: November 2, 2016
This is version 144 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, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.