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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1)
Status
Reviewed-Annotation score: 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: 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 sitei292NADUniRule annotation1
Metal bindingi345Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi347Potassium; via carbonyl oxygenUniRule annotation1
Binding sitei348IMPUniRule annotation1
Active sitei350Thioimidate intermediateUniRule annotation1
Metal bindingi350Potassium; via carbonyl oxygenUniRule annotation1
Active sitei446Proton acceptorUniRule annotation1
Binding sitei460IMPUniRule annotation1
Metal bindingi514Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi516Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi343 – 345NADUniRule 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

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:RB11822
OrganismiRhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1)
Taxonomic identifieri243090 [NCBI]
Taxonomic lineageiBacteriaPlanctomycetesPlanctomycetiaPlanctomycetalesPlanctomycetaceaeRhodopirellula
Proteomesi
  • UP000001025 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004156901 – 539Inosine-5'-monophosphate dehydrogenaseAdd BLAST539

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi243090.RB11822.

Structurei

3D structure databases

ProteinModelPortaliQ7UJL3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini140 – 196CBS 1UniRule annotationAdd BLAST57
Domaini200 – 257CBS 2UniRule annotationAdd BLAST58

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni383 – 385IMP bindingUniRule annotation3
Regioni406 – 407IMP bindingUniRule annotation2
Regioni430 – 434IMP 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.
HOGENOMiHOG000165755.
InParanoidiQ7UJL3.
KOiK00088.
OMAiSSMGYCG.
OrthoDBiPOG091H02IM.

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.

Q7UJL3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGASTRFRRQ SGKVPYNSTA ASVIIARFPH RITFGCPRPR GNENGMFDDK
60 70 80 90 100
IGDLGVTFDD VLLQPRYSEV VPSEVDVSSQ MTQRIRLQIP LISSPMDTVT
110 120 130 140 150
ESEMAIALAK EGGLGIVHKN LSVRRQTEEV LKVKRSANGI IVNPVTLNPA
160 170 180 190 200
QKVSAAAELM DRANVSGIPI VEDDRTLAGI LTRRDLRFLE DPDMPISQVM
210 220 230 240 250
TRENLVTAVG NVTLAQAEKI LTEKRVEKLL LIDEERKLTG LITIRDIDMM
260 270 280 290 300
KRYPRACKDP QGRLRVGAAI GVGDYERAES LIGKGVDVLV VDSAHGHSRN
310 320 330 340 350
VIETVREIKQ NKSWDIDVVA GNVATAEGAA DLIAAGADAV KVGIGPGSIC
360 370 380 390 400
TTRVISGIGV PQVTAILSAV KVAQEKNIPV IADGGIRFSG DITKAIAAGA
410 420 430 440 450
STVMIGSLFA GLAESPGKMI LYQGRTFKAY RGMGSMGAMV KGSSDRYRQK
460 470 480 490 500
GTEAGKLVPE GVEGRVPFKG PLSDYAYQLV GGLRAGMGYV GTRTIEELRR
510 520 530
DAKFIRVSAA TVRENHPHDI AITQEAPNYS PDVHSGDAG
Length:539
Mass (Da):57,876
Last modified:October 1, 2003 - v1
Checksum:i7090A0C1A9075141
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX294154 Genomic DNA. Translation: CAD77245.1.
RefSeqiNP_870170.1. NC_005027.1.
WP_011123443.1. NC_005027.1.

Genome annotation databases

EnsemblBacteriaiCAD77245; CAD77245; RB11822.
GeneIDi1795246.
KEGGirba:RB11822.
PATRICi23252947. VBIRhoBal59814_5703.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX294154 Genomic DNA. Translation: CAD77245.1.
RefSeqiNP_870170.1. NC_005027.1.
WP_011123443.1. NC_005027.1.

3D structure databases

ProteinModelPortaliQ7UJL3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243090.RB11822.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAD77245; CAD77245; RB11822.
GeneIDi1795246.
KEGGirba:RB11822.
PATRICi23252947. VBIRhoBal59814_5703.

Phylogenomic databases

eggNOGiENOG4105CP4. Bacteria.
COG0516. LUCA.
COG0517. LUCA.
HOGENOMiHOG000165755.
InParanoidiQ7UJL3.
KOiK00088.
OMAiSSMGYCG.
OrthoDBiPOG091H02IM.

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.
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_RHOBA
AccessioniPrimary (citable) accession number: Q7UJL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: October 1, 2003
Last modified: November 2, 2016
This is version 93 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

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.