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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Acinetobacter calcoaceticus
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), Inosine-5'-monophosphate dehydrogenase (guaB_2), Inosine-5'-monophosphate dehydrogenase (guaB), 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 sitei247NADUniRule annotation1
Metal bindingi299Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi301Potassium; via carbonyl oxygenUniRule annotation1
Binding sitei302IMPUniRule annotation1
Active sitei304Thioimidate intermediateUniRule annotation1
Metal bindingi304Potassium; via carbonyl oxygenUniRule annotation1
Active sitei401Proton 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 bindingi297 – 299NADUniRule 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
OrganismiAcinetobacter calcoaceticus
Taxonomic identifieri471 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000936881 – 488Inosine-5'-monophosphate dehydrogenaseAdd BLAST488

Proteomic databases

PRIDEiP31002.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi871585.BDGL_002788.

Structurei

3D structure databases

ProteinModelPortaliP31002.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini93 – 148CBS 1UniRule annotationAdd BLAST56
Domaini152 – 210CBS 2UniRule annotationAdd BLAST59

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni336 – 338IMP bindingUniRule annotation3
Regioni359 – 360IMP bindingUniRule annotation2
Regioni383 – 387IMP 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.

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.

P31002-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTIVQEALT FDDVLLLPAY STVLPKDVSL KTRLTRGIYL NIPLVSAAMD
60 70 80 90 100
TVTESRMAIA MAQNGGIGIL HKNMDIAAQA AEVRRVKKFE AGMVKDPITV
110 120 130 140 150
SPETTVRELI AITSANNISG VPVVKDSKVV GIVTGRDTRF ETNLEQPVSN
160 170 180 190 200
IMTGQDRLVT VREGESKENI QALLQKHRIE KVLVVGESNE LKGLITVTDF
210 220 230 240 250
RKAESYPNSC KDDLGRLRVG AAVGTGADTP SRVEALVEAG VDVIVVDTAH
260 270 280 290 300
GHSAGVIERV RWVKQNFPQV QVIGGNIATG DAALALLDAG ADAVKVGIGP
310 320 330 340 350
GSICTTRIVA GIGMPQISAI DSVASALKDQ IPLIADGGIP FSGDMAKAIG
360 370 380 390 400
AGASTIMVGS LLAGTEEAPG EVEFFQGRYY KAYRGMGSLG AMAGRTGSAD
410 420 430 440 450
RYFQDSKAGA EKLVPEGIEG RVPYKGPMGN IVHQMMGGLR SSMGYTGSAV
460 470 480
IEDLRQNAKF VKITSAGMSE SHVHDVTITK EAPNYRVG
Length:488
Mass (Da):51,530
Last modified:July 1, 1993 - v1
Checksum:i3DE0F8F9B5157A03
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66859 Genomic DNA. Translation: CAA47328.1.
PIRiS23226.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66859 Genomic DNA. Translation: CAA47328.1.
PIRiS23226.

3D structure databases

ProteinModelPortaliP31002.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi871585.BDGL_002788.

Proteomic databases

PRIDEiP31002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CP4. Bacteria.
COG0516. LUCA.
COG0517. LUCA.

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_ACICA
AccessioniPrimary (citable) accession number: P31002
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: October 5, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.