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Q9KTW3

- Q9KTW3_VIBCH

UniProt

Q9KTW3 - Q9KTW3_VIBCH

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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Unreviewed - Annotation score: 3 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

Note: Potassium.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 sitei256 – 2561NADImported
Binding sitei279 – 2791NADImported
Metal bindingi302 – 3021Potassium; via carbonyl oxygenUniRule annotation
Metal bindingi304 – 3041Potassium; via carbonyl oxygenUniRule annotation
Binding sitei305 – 3051IMPUniRule annotation
Active sitei307 – 3071Thioimidate intermediateUniRule annotation
Metal bindingi307 – 3071Potassium; via carbonyl oxygenUniRule annotation
Binding sitei417 – 4171IMPUniRule annotation
Binding sitei442 – 4421NADImported
Metal bindingi471 – 4711Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi472 – 4721Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
Metal bindingi473 – 4731Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi250 – 2523NADUniRule annotationImported
Nucleotide bindingi300 – 3023NADUniRule annotationImported

GO - Molecular functioni

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

GO - Biological processi

  1. GMP biosynthetic process Source: UniProtKB-HAMAP
  2. purine ribonucleotide biosynthetic process Source: TIGR
Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotation

Keywords - Biological processi

GMP biosynthesisUniRule annotation, Purine biosynthesis

Keywords - Ligandi

Metal-bindingUniRule annotation, NADUniRule annotation, Nucleotide-bindingImported, PotassiumUniRule annotation

Enzyme and pathway databases

BioCyciVCHO:VC0767-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
Gene namesi
Name:guaBUniRule annotation
Ordered Locus Names:VC_0767Imported
OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)Imported
Taxonomic identifieri243277 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
ProteomesiUP000000584: Chromosome 1

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi243277.VC0767.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FEZX-ray2.16A/B1-92[»]
A/B200-489[»]
4FO4X-ray2.03A/B1-90[»]
A/B220-489[»]
4FXSX-ray2.24A1-489[»]
4IX2X-ray2.15A/B/C/D1-90[»]
A/B/C/D220-489[»]
4QNEX-ray2.32A/B1-90[»]
A/B220-489[»]
4QQ3X-ray1.72A1-90[»]
A220-489[»]
ProteinModelPortaliQ9KTW3.
SMRiQ9KTW3. Positions 5-487.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini95 – 15460CBS 1UniRule annotationAdd
BLAST
Domaini155 – 21662CBS 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni340 – 3423IMP bindingUniRule annotation
Regioni363 – 3642IMP bindingUniRule annotation
Regioni387 – 3915IMP bindingUniRule annotation

Sequence similaritiesi

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

Keywords - Domaini

CBS domainUniRule annotation, RepeatUniRule annotation

Phylogenomic databases

KOiK00088.
OMAiHGHSKNI.
OrthoDBiEOG6GTZPV.

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.

Q9KTW3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHMLRIAKEA LTFDDVLLVP AHSTVLPNTA DLRTRLTKNI ALNIPMVSAS
60 70 80 90 100
MDTVTEARLA IALAQEGGIG FIHKNMSIEQ QAAQVHQVKI FEAGVVTHPV
110 120 130 140 150
TVRPEQTIAD VMELTHYHGF AGFPVVTENN ELVGIITGRD VRFVTDLTKS
160 170 180 190 200
VAAVMTPKER LATVKEGATG AEVQEKMHKA RVEKILVVND EFQLKGMITA
210 220 230 240 250
KDFHKAESKP NACKDEQGRL RVGAAVGAAP GNEERVKALV EAGVDVLLID
260 270 280 290 300
SSHGHSEGVL QRIRETRAAY PHLEIIGGNV ATAEGARALI EAGVSAVKVG
310 320 330 340 350
IGPGSICTTR IVTGVGVPQI TAIADAAGVA NEYGIPVIAD GGIRFSGDIS
360 370 380 390 400
KAIAAGASCV MVGSMFAGTE EAPGEVILYQ GRSYKAYRGM GSLGAMSKGS
410 420 430 440 450
SDRYFQTDNA ADKLVPEGIE GRIAYKGHLK EIIHQQMGGL RSCMGLTGSA
460 470 480
TVEDLRTKAQ FVRISGAGMK ESHVHDVQIT KEAPNYRLG
Length:489
Mass (Da):51,943
Last modified:October 1, 2000 - v1
Checksum:iB38133B52F8661C4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003852 Genomic DNA. Translation: AAF93932.1.
PIRiC82282.
RefSeqiNP_230416.1. NC_002505.1.

Genome annotation databases

EnsemblBacteriaiAAF93932; AAF93932; VC_0767.
GeneIDi2615310.
KEGGivch:VC0767.
PATRICi20080645. VBIVibCho83274_0731.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003852 Genomic DNA. Translation: AAF93932.1 .
PIRi C82282.
RefSeqi NP_230416.1. NC_002505.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4FEZ X-ray 2.16 A/B 1-92 [» ]
A/B 200-489 [» ]
4FO4 X-ray 2.03 A/B 1-90 [» ]
A/B 220-489 [» ]
4FXS X-ray 2.24 A 1-489 [» ]
4IX2 X-ray 2.15 A/B/C/D 1-90 [» ]
A/B/C/D 220-489 [» ]
4QNE X-ray 2.32 A/B 1-90 [» ]
A/B 220-489 [» ]
4QQ3 X-ray 1.72 A 1-90 [» ]
A 220-489 [» ]
ProteinModelPortali Q9KTW3.
SMRi Q9KTW3. Positions 5-487.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243277.VC0767.

Protocols and materials databases

DNASUi 2615310.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAF93932 ; AAF93932 ; VC_0767 .
GeneIDi 2615310.
KEGGi vch:VC0767.
PATRICi 20080645. VBIVibCho83274_0731.

Phylogenomic databases

KOi K00088.
OMAi HGHSKNI.
OrthoDBi EOG6GTZPV.

Enzyme and pathway databases

UniPathwayi UPA00601 ; UER00295 .
BioCyci VCHO:VC0767-MONOMER.

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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 39315 / El Tor Inaba N16961Imported.
  2. "Inosine 5'-monophosphate dehydrogenase from Vibrio cholerae, deletion mutant."
    Osipiuk J., Maltseva N., Makowska-Grzyska M., Gu M., Anderson W.F., Joachimiak A.
    Submitted (MAY-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 1-92 AND 200-489.
  3. "Inosine 5'-monophosphate dehydrogenase from Vibrio cholerae, deletion mutant, complexed with IMP and mycophenolic acid."
    Osipiuk J., Maltseva N., Makowska-Grzyska M., Gu M., Anderson W.F., Joachimiak A.
    Submitted (JUN-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 1-90 AND 220-489.
  4. "Inosine 5'-monophosphate dehydrogenase from Vibrio cholerae complexed with IMP and mycophenolic acid."
    Osipiuk J., Maltseva N., Makowska-Grzyska M., Jedrzejczak R., Anderson W.F., Joachimiak A.
    Submitted (JUL-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS).
  5. "Inosine 5'-monophosphate dehydrogenase from Vibrio cholerae, deletion mutant, complexed with IMP."
    Osipiuk J., Maltseva N., Makowska-Grzyska M., Gu M., Anderson W.F., Joachimiak A.
    Submitted (JAN-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-90 AND 220-489.
  6. "Inosine 5'-monophosphate dehydrogenase from Vibrio cholerae, deletion mutant, in complex with NAD and IMP."
    Osipiuk J., Maltseva N., Makowska-Grzyska M., Gu M., Anderson W.F., Joachimiak A.
    Submitted (JUN-2014) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 1-90 AND 220-489 IN COMPLEX WITH NAD.
  7. "Inosine 5'-monophosphate dehydrogenase from vibrio cholerae, deletion mutant, in complex with xmp."
    Osipiuk J., Maltseva N., Makowska-Grzyska M., Gu M., Anderson W.F., Joachimiak A.
    Submitted (JUN-2014) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 1-90 AND 220-489.

Entry informationi

Entry nameiQ9KTW3_VIBCH
AccessioniPrimary (citable) accession number: Q9KTW3
Entry historyi
Integrated into UniProtKB/TrEMBL: October 1, 2000
Last sequence update: October 1, 2000
Last modified: November 26, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported, Complete proteome, Reference proteomeImported

External Data

Dasty 3