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A4XBG8 (A4XBG8_SALTO) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 47. 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:Strop_3837
OrganismSalinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440) [Complete proteome] [HAMAP] EMBL ABP56267.1
Taxonomic identifier369723 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micromonosporineae › Micromonosporaceae › Salinispora ›

Protein attributes

Sequence length520 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. 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. HAMAP-Rule MF_01964 RuleBase RU003927

Contains 2 CBS domains. HAMAP-Rule MF_01964

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain121 – 18060CBS 1 By similarity HAMAP-Rule MF_01964
Domain181 – 23858CBS 2 By similarity HAMAP-Rule MF_01964
Nucleotide binding324 – 3263NAD By similarity HAMAP-Rule MF_01964
Region364 – 3663IMP binding By similarity HAMAP-Rule MF_01964
Region387 – 3882IMP binding By similarity HAMAP-Rule MF_01964
Region411 – 4155IMP binding By similarity HAMAP-Rule MF_01964

Sites

Active site3311Thioimidate intermediate By similarity PIRSR PIRSR000130-1 HAMAP-Rule MF_01964
Metal binding3261Potassium; via carbonyl oxygen By similarity HAMAP-Rule MF_01964
Metal binding3281Potassium; via carbonyl oxygen By similarity HAMAP-Rule MF_01964
Metal binding3311Potassium; via carbonyl oxygen By similarity HAMAP-Rule MF_01964
Metal binding5021Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity HAMAP-Rule MF_01964
Metal binding5031Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity HAMAP-Rule MF_01964
Metal binding5041Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity HAMAP-Rule MF_01964
Binding site2751NAD By similarity HAMAP-Rule MF_01964
Binding site4481IMP By similarity HAMAP-Rule MF_01964

Sequences

Sequence LengthMass (Da)Tools
A4XBG8 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 0317B165C862CC0C

FASTA52054,440
        10         20         30         40         50         60 
MENSPSTVQP TDADNGELGG HLPELPAGSA RVVPLGLTFD DVLLQPGGSD VVPSRVNTRT 

        70         80         90        100        110        120 
KLTRTVELNI PLLSSAMDTV TEGRMAIAMA RQGGIGVLHR NLSVEDQALQ VDLVKRSESG 

       130        140        150        160        170        180 
MITNPVTAGP DDTLQDVDTL CGQYRISGVP VVDGDGQLVG IVTNRDMRFV SDPATPVREI 

       190        200        210        220        230        240 
MTRTPLVTAP VGVSKEDALG LLQQHKVEKL PIVDGAGKLR GLITVKDFTK SEQYPNATKD 

       250        260        270        280        290        300 
SAGRLRVAAA VGVGEDAYKR ARALVDAGVD VLIVDTAHGH QRAVLEMVAR IKKDASVDVV 

       310        320        330        340        350        360 
GGNVATYAGA KALIEAGVDG VKVGVGPGAI CTTRIVAGVG VPQVTAIMEA ARAARPAGVP 

       370        380        390        400        410        420 
VIGDGGIQYS GDIAKALVAG ADTVMLGGLL AGCAESPGEL IFINGKQYKA YRGMGSLGAM 

       430        440        450        460        470        480 
QSRGQVRSYS KDRYFQQDVT SDDKLVPEGV EGQVPYRGPL AQVAHQLVGG LRLAMGYAGA 

       490        500        510        520 
ESVSELHRRG QLIRITAAGL KESHPHDIQM VAEAPNYHTR

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References

[1]"Complete sequence of Salinispora tropica CNB-440."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sun H., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Jensen P.R., Moore B.S., Udwary D.W., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-916 / DSM 44818 / CNB-440.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000667 Genomic DNA. Translation: ABP56267.1.
RefSeqYP_001160645.1. NC_009380.1.

3D structure databases

ProteinModelPortalA4XBG8.
ModBaseSearch...

Protein-protein interaction databases

STRING369723.Strop_3837.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP56267; ABP56267; Strop_3837.
GeneID5060315.
KEGGstp:Strop_3837.
PATRIC23446866. VBISalTro43511_3961.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0517.
HOGENOMHOG000165755.
KOK00088.
OMASAGLKES.
ProtClustDBCLSK969838.

Enzyme and pathway databases

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.
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.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA4XBG8_SALTO
AccessionPrimary (citable) accession number: A4XBG8
Entry history
Integrated into UniProtKB/TrEMBL: May 29, 2007
Last sequence update: May 29, 2007
Last modified: May 1, 2013
This is version 47 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