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Q9KH33

- IMDH_RHITR

UniProt

Q9KH33 - IMDH_RHITR

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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Rhizobium tropici
Status
Reviewed - 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei253 – 2531NADUniRule annotation
Metal bindingi305 – 3051Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi307 – 3071Potassium; via carbonyl oxygenUniRule annotation
Binding sitei308 – 3081IMPUniRule annotation
Active sitei310 – 3101Thioimidate intermediateUniRule annotation
Metal bindingi310 – 3101Potassium; via carbonyl oxygenUniRule annotation
Binding sitei421 – 4211IMPUniRule annotation
Metal bindingi475 – 4751Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi476 – 4761Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi477 – 4771Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi303 – 3053NADUniRule annotation

GO - Molecular functioni

  1. adenyl nucleotide binding Source: InterPro
  2. IMP dehydrogenase activity Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. GMP biosynthetic process Source: UniProtKB-HAMAP
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 498498Inosine-5'-monophosphate dehydrogenasePRO_0000093704Add
BLAST

Proteomic databases

PRIDEiQ9KH33.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ9KH33.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini98 – 15558CBS 1UniRule annotationAdd
BLAST
Domaini159 – 21658CBS 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni343 – 3453IMP bindingUniRule annotation
Regioni366 – 3672IMP bindingUniRule annotation
Regioni390 – 3945IMP bindingUniRule annotation

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

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH.
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. 1 hit.
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.

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

ProteinModelPortali Q9KH33.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q9KH33.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00601 ; UER00295 .

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_01964. IMPDH.
InterProi IPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view ]
PANTHERi PTHR11911:SF6. PTHR11911:SF6. 1 hit.
Pfami PF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000130. IMPDH. 1 hit.
SMARTi SM00116. CBS. 2 hits.
[Graphical view ]
TIGRFAMsi TIGR01302. IMP_dehydrog. 1 hit.
PROSITEi PS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "A guaB mutant strain of Rhizobium tropici CIAT899 pleiotropically defective in thermal tolerance and symbiosis."
    Riccillo P.M., Collavino M.M., Grasso D.H., England R., de Bruijn F.J., Aguilar O.M.
    Mol. Plant Microbe Interact. 13:1228-1236(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 899.

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: November 26, 2014
This is version 83 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

External Data

Dasty 3