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Q9KTW3 (Q9KTW3_VIBCH) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964

Short name=IMP dehydrogenase HAMAP-Rule MF_01964
Short name=IMPD HAMAP-Rule MF_01964
Short name=IMPDH HAMAP-Rule MF_01964
EC=1.1.1.205 HAMAP-Rule MF_01964
Gene names
Name:guaB HAMAP-Rule MF_01964
Ordered Locus Names:VC_0767 EMBL AAF93932.1
OrganismVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP] EMBL AAF93932.1
Taxonomic identifier243277 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length489 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_01964

Catalytic activity

Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH. HAMAP-Rule MF_01964

Cofactor

Potassium By similarity. HAMAP-Rule MF_01964

Enzyme regulation

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 By similarity. HAMAP-Rule MF_01964

Pathway

Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. HAMAP-Rule MF_01964

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_01964

Sequence similarities

Belongs to the IMPDH/GMPR family. RuleBase RU003927 HAMAP-Rule MF_01964

Contains 2 CBS domains. HAMAP-Rule MF_01964

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain95 – 15460CBS 1 By similarity HAMAP-Rule MF_01964
Domain155 – 21662CBS 2 By similarity HAMAP-Rule MF_01964
Nucleotide binding250 – 2523NAD PDB 4HLV
Nucleotide binding250 – 2523NAD By similarity HAMAP-Rule MF_01964
Nucleotide binding300 – 3023NAD PDB 4HLV
Nucleotide binding300 – 3023NAD By similarity HAMAP-Rule MF_01964
Region340 – 3423IMP binding By similarity HAMAP-Rule MF_01964
Region363 – 3642IMP binding By similarity HAMAP-Rule MF_01964
Region387 – 3915IMP binding By similarity HAMAP-Rule MF_01964

Sites

Active site3071Thioimidate intermediate By similarity PIRSR PIRSR000130-1 HAMAP-Rule MF_01964
Metal binding3021Potassium 1; via carbonyl oxygen PDB 4FO4 PDB 4FXS PDB 4HLV
Metal binding3021Potassium 2; via carbonyl oxygen PDB 4IX2
Metal binding3021Potassium; via carbonyl oxygen By similarity HAMAP-Rule MF_01964
Metal binding3041Potassium 1; via carbonyl oxygen PDB 4FO4 PDB 4FXS PDB 4HLV
Metal binding3041Potassium 2; via carbonyl oxygen PDB 4IX2
Metal binding3041Potassium; via carbonyl oxygen By similarity HAMAP-Rule MF_01964
Metal binding3071Potassium 1; via carbonyl oxygen PDB 4FO4 PDB 4FXS PDB 4HLV
Metal binding3071Potassium 2; via carbonyl oxygen PDB 4IX2
Metal binding3071Potassium; via carbonyl oxygen By similarity HAMAP-Rule MF_01964
Metal binding4711Potassium 1; via carbonyl oxygen PDB 4FO4 PDB 4FXS PDB 4HLV
Metal binding4711Potassium 3; via carbonyl oxygen PDB 4IX2
Metal binding4711Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity HAMAP-Rule MF_01964
Metal binding4721Potassium 1; via carbonyl oxygen PDB 4FO4 PDB 4FXS PDB 4HLV
Metal binding4721Potassium 3; via carbonyl oxygen PDB 4IX2
Metal binding4721Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity HAMAP-Rule MF_01964
Metal binding4731Potassium 1; via carbonyl oxygen PDB 4FO4 PDB 4FXS PDB 4HLV
Metal binding4731Potassium 3; via carbonyl oxygen PDB 4IX2
Metal binding4731Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity HAMAP-Rule MF_01964
Binding site2561NAD PDB 4HLV
Binding site2791NAD PDB 4HLV
Binding site3051IMP By similarity HAMAP-Rule MF_01964
Binding site4171IMP By similarity HAMAP-Rule MF_01964
Binding site4421NAD PDB 4HLV

Sequences

Sequence LengthMass (Da)Tools
Q9KTW3 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: B38133B52F8661C4

FASTA48951,943
        10         20         30         40         50         60 
MHMLRIAKEA LTFDDVLLVP AHSTVLPNTA DLRTRLTKNI ALNIPMVSAS MDTVTEARLA 

        70         80         90        100        110        120 
IALAQEGGIG FIHKNMSIEQ QAAQVHQVKI FEAGVVTHPV TVRPEQTIAD VMELTHYHGF 

       130        140        150        160        170        180 
AGFPVVTENN ELVGIITGRD VRFVTDLTKS VAAVMTPKER LATVKEGATG AEVQEKMHKA 

       190        200        210        220        230        240 
RVEKILVVND EFQLKGMITA KDFHKAESKP NACKDEQGRL RVGAAVGAAP GNEERVKALV 

       250        260        270        280        290        300 
EAGVDVLLID SSHGHSEGVL QRIRETRAAY PHLEIIGGNV ATAEGARALI EAGVSAVKVG 

       310        320        330        340        350        360 
IGPGSICTTR IVTGVGVPQI TAIADAAGVA NEYGIPVIAD GGIRFSGDIS KAIAAGASCV 

       370        380        390        400        410        420 
MVGSMFAGTE EAPGEVILYQ GRSYKAYRGM GSLGAMSKGS SDRYFQTDNA ADKLVPEGIE 

       430        440        450        460        470        480 
GRIAYKGHLK EIIHQQMGGL RSCMGLTGSA TVEDLRTKAQ FVRISGAGMK ESHVHDVQIT 


KEAPNYRLG 

« Hide

References

« Hide 'large scale' references
[1]"DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae."
Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S. expand/collapse author list , Qin H., Dragoi I., Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.
Nature 406:477-483(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39315 / El Tor Inaba N16961.
[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 IN COMPLEX WITH POTASSIUM.
[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) IN COMPLEX WITH POTASSIUM.
[5]"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 (OCT-2012) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 1-90 AND 220-489 IN COMPLEX WITH NAD AND POTASSIUM.
[6]"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 IN COMPLEX WITH POTASSIUM.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE003852 Genomic DNA. Translation: AAF93932.1.
PIRC82282.
RefSeqNP_230416.1. NC_002505.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4FEZX-ray2.16A/B1-92[»]
A/B200-489[»]
4FO4X-ray2.03A/B1-90[»]
A/B220-489[»]
4FXSX-ray2.24A1-489[»]
4HLVX-ray2.32A/B1-90[»]
A/B220-489[»]
4IX2X-ray2.15A/B/C/D1-90[»]
A/B/C/D220-489[»]
ProteinModelPortalQ9KTW3.
SMRQ9KTW3. Positions 5-487.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243277.VC0767.

Protocols and materials databases

DNASU2615310.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF93932; AAF93932; VC_0767.
GeneID2615310.
KEGGvch:VC0767.
PATRIC20080645. VBIVibCho83274_0731.

Phylogenomic databases

KOK00088.
OMAHGHSKNI.
OrthoDBEOG6GTZPV.

Enzyme and pathway databases

BioCycVCHO:VC0767-MONOMER.
UniPathwayUPA00601; UER00295.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01964. IMPDH.
InterProIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PANTHERPTHR11911:SF6. PTHR11911:SF6. 1 hit.
PfamPF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFPIRSF000130. IMPDH. 1 hit.
SMARTSM00116. CBS. 2 hits.
[Graphical view]
TIGRFAMsTIGR01302. IMP_dehydrog. 1 hit.
PROSITEPS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ9KTW3_VIBCH
AccessionPrimary (citable) accession number: Q9KTW3
Entry history
Integrated into UniProtKB/TrEMBL: October 1, 2000
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)