Skip Header

Contribute Send feedback
Read comments (?) or add your own

A8ZSF3 (A8ZSF3_DESOH) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

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:Dole_1886
OrganismDesulfococcus oleovorans (strain DSM 6200 / Hxd3) [Complete proteome] [HAMAP] EMBL ABW67690.1
Taxonomic identifier96561 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Desulfobacterales › Desulfobacteraceae › Desulfococcus ›

Protein attributes

Sequence length485 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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. RuleBase RU003928 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. RuleBase RU003928 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

Domain93 – 14856CBS 1 By similarity HAMAP-Rule MF_01964
Domain152 – 21160CBS 2 By similarity HAMAP-Rule MF_01964
Nucleotide binding295 – 2973NAD By similarity HAMAP-Rule MF_01964
Region335 – 3373IMP binding By similarity HAMAP-Rule MF_01964
Region358 – 3592IMP binding By similarity HAMAP-Rule MF_01964
Region382 – 3865IMP binding By similarity HAMAP-Rule MF_01964

Sites

Active site3021Thioimidate intermediate By similarity PIRSR PIRSR000130-1 HAMAP-Rule MF_01964
Metal binding2971Potassium; via carbonyl oxygen By similarity HAMAP-Rule MF_01964
Metal binding2991Potassium; via carbonyl oxygen By similarity HAMAP-Rule MF_01964
Metal binding3021Potassium; via carbonyl oxygen By similarity HAMAP-Rule MF_01964
Metal binding4671Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity HAMAP-Rule MF_01964
Metal binding4681Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity HAMAP-Rule MF_01964
Metal binding4691Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity HAMAP-Rule MF_01964
Binding site2451NAD By similarity HAMAP-Rule MF_01964
Binding site3001IMP By similarity HAMAP-Rule MF_01964
Binding site4131IMP By similarity HAMAP-Rule MF_01964

Sequences

Sequence LengthMass (Da)Tools
A8ZSF3 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 7E7BBE800D76735F

FASTA48551,870
        10         20         30         40         50         60 
MKITPEETYS FDDVLLIPNY SDVLPDDVNT TTRLTVELSV NIPIVSAAMD TVTESATAIS 

        70         80         90        100        110        120 
MARAGGLGFI HRNMSIEAQA IEVGKVKKSE SGMIVDPVTT GPNEPISAVL SLMKEYNISG 

       130        140        150        160        170        180 
VPVVQGDKLV GIVTNRDLRF EGDLDRKVSE VMTSKLITVP EGITLEESKE LLHRHKIEKL 

       190        200        210        220        230        240 
LVVDKKGRLA GMITMKDIEK LKKYPNSCKD ELGRLRVGAA IGVGKEAMER AEALLKAGAD 

       250        260        270        280        290        300 
VIVIDTSHGH SQNVIDTVKT LKQTFKPIQV IAGNVCTAKG AEALIEAGVD GVKIGVGPGS 

       310        320        330        340        350        360 
ICTTRIVAGV GMPQLTAILN CRSVSNKTGV PLIADGGIKY SGDITKALAA GAHTVMLGGL 

       370        380        390        400        410        420 
LAGTEESPGE TILFQGRSYK VYRGMGSVEA MKQGSKDRYY QTNEVEDSQL VPEGIVGRIP 

       430        440        450        460        470        480 
YRGTVSGNIT QLVGGLKAGM GYLGCRNVDE LRERGRFVKI SAAGLRESHV HDVIITKEAP 


NYRVD

« Hide

References

[1]"Complete sequence of Desulfococcus oleovorans Hxd3."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Wawrik B., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 6200 / Hxd3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000859 Genomic DNA. Translation: ABW67690.1.
RefSeqYP_001529767.1. NC_009943.1.

3D structure databases

ProteinModelPortalA8ZSF3.
SMRA8ZSF3. Positions 5-483.
ModBaseSearch...

Protein-protein interaction databases

STRING96561.Dole_1886.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABW67690; ABW67690; Dole_1886.
GeneID5694726.
KEGGdol:Dole_1886.
PATRIC21693885. VBIDesOle35880_1947.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0517.
HOGENOMHOG000165755.
KOK00088.
OMASAGLKES.
ProtClustDBCLSK2402146.

Enzyme and pathway databases

BioCycDOLE96561:GHF3-1937-MONOMER.
UniPathwayUPA00601; UER00295.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01964. IMPDH.
InterProIPR013785. Aldolase_TIM.
IPR000644. Cysta_beta_synth_core.
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 nameA8ZSF3_DESOH
AccessionPrimary (citable) accession number: A8ZSF3
Entry history
Integrated into UniProtKB/TrEMBL: January 15, 2008
Last sequence update: January 15, 2008
Last modified: May 1, 2013
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info