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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Rhizobium tropici
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 sitei253NADUniRule annotation1
Metal bindingi305Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi307Potassium; via carbonyl oxygenUniRule annotation1
Binding sitei308IMPUniRule annotation1
Active sitei310Thioimidate intermediateUniRule annotation1
Metal bindingi310Potassium; via carbonyl oxygenUniRule annotation1
Active sitei406Proton acceptorUniRule annotation1
Binding sitei421IMPUniRule annotation1
Metal bindingi475Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi476Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi477Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi303 – 305NADUniRule 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
OrganismiRhizobium tropici
Taxonomic identifieri398 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000937041 – 498Inosine-5'-monophosphate dehydrogenaseAdd BLAST498

Proteomic databases

PRIDEiQ9KH33.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ9KH33.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini98 – 155CBS 1UniRule annotationAdd BLAST58
Domaini159 – 216CBS 2UniRule annotationAdd BLAST58

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni343 – 345IMP bindingUniRule annotation3
Regioni366 – 367IMP bindingUniRule annotation2
Regioni390 – 394IMP bindingUniRule annotation5

Sequence similaritiesi

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

Keywords - Domaini

CBS domain, Repeat

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. 1 hit.
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.

Q9KH33-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARIIETSTG LDALTFDDVL LQPGHSEVMP GQTNIATRIA QDIELNVPIL
60 70 80 90 100
SAAMDTVTES RLAIAMAQAG GMGVIHRNLT PVQQAEEVRQ VKKFESGMVV
110 120 130 140 150
NPVTIGPDAT LAEALSLDEG PRHFRASPVV EKSHRLVGIL TNRDVRFASD
160 170 180 190 200
PEQKIYELMT RENLVTVKDG VQQHEAKRLL HTHRIEKXLV VDADSRFVGL
210 220 230 240 250
ITVKDIEKSQ LNPHASKDAQ GRLRAAAAIS VGDDGYERAE RLIDAGVDLL
260 270 280 290 300
VVDTAHGHSQ RVLDAVTRVK KLSNSVRIMA GNVATYDGTR ALIDAGADAV
310 320 330 340 350
KVGIGPGSIC TTRIVAGVGV PQLAAIMSAV QAAQDQNIPI IADGGIKFSG
360 370 380 390 400
DLAKAIAAGA SAAMIGSLLA GTDESPGEVY LYQGRSFKAY RGMGSVGAMA
410 420 430 440 450
RGSADRYFQA EVRDTLKLVP EGIEGXVPYK GPVSGVLHQL AGGLKAAMGY
460 470 480 490
VGGADLKDFQ ERATFVRISG AGLRESHAHD VTITPRKARI IPAQAADR
Length:498
Mass (Da):52,838
Last modified:October 1, 2000 - v1
Checksum:i0A99E38B1078ED73
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF272827 Genomic DNA. Translation: AAF85967.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF272827 Genomic DNA. Translation: AAF85967.1.

3D structure databases

ProteinModelPortaliQ9KH33.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ9KH33.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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. 1 hit.
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_RHITR
AccessioniPrimary (citable) accession number: Q9KH33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 1, 2000
Last modified: September 7, 2016
This is version 89 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.