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A5EYL9 (GUAC_VIBC3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
GMP reductase

EC=1.7.1.7
Alternative name(s):
Guanosine 5'-monophosphate oxidoreductase
Short name=Guanosine monophosphate reductase
Gene names
Name:guaC
Ordered Locus Names:VC0395_1080, VC395_A0188
OrganismVibrio cholerae serotype O1 (strain ATCC 39541 / Ogawa 395 / O395) [Complete proteome] [HAMAP]
Taxonomic identifier345073 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length347 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides By similarity. HAMAP-Rule MF_00596

Catalytic activity

Inosine 5'-phosphate + NH3 + NADP+ = guanosine 5'-phosphate + NADPH. HAMAP-Rule MF_00596

Subunit structure

Homotetramer By similarity.

Sequence similarities

Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily.

Ontologies

Keywords
   LigandMetal-binding
NADP
Potassium
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpurine nucleotide metabolic process

Inferred from electronic annotation. Source: HAMAP

   Molecular_functionGMP reductase activity

Inferred from electronic annotation. Source: HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 347347GMP reductase HAMAP-Rule MF_00596
PRO_1000072625

Regions

Nucleotide binding108 – 13124NADP By similarity
Nucleotide binding216 – 23924NADP; ribose moiety By similarity

Sites

Active site1861Thioimidate intermediate By similarity
Metal binding1811Potassium; via carbonyl oxygen By similarity
Metal binding1831Potassium; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
A5EYL9 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 574F76175FF4652E

FASTA34737,114
        10         20         30         40         50         60 
MRIEQELKLG FKDVLFRPKR STLKSRSQVN LTREFTFKHS GRQWSGVPVI AANMDSVGSF 

        70         80         90        100        110        120 
AMAKALAEHG VMTAVHKHYT VADWAEFVKS ADKATLNNVM VSTGTSEADF QKTKDVMALS 

       130        140        150        160        170        180 
DELIFICIDI ANGYSEHLVE YVQRVRAAFP DKVISAGNVV TGDMVEELIL AGADIVKVGI 

       190        200        210        220        230        240 
GPGSVCTTRV KTGVGYPQLS AIIECADAAH GLGGRIIGDG GCTCPGDVAK AFGGGADFVM 

       250        260        270        280        290        300 
LGGMLAGHEE AGGELIVKDG ETFMKFYGMS SKSAMDKHSG GVAGYRAAEG KTVLLPYRGS 

       310        320        330        340 
VHGTIQDILG GVRSTCTYVG AAELRELTKR TTFIRVQEQE NNVYGRE 

« Hide

References

[1]Heidelberg J.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39541 / Ogawa 395 / O395.
[2]"A recalibrated molecular clock and independent origins for the cholera pandemic clones."
Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., Wang W., Wang J., Qian W., Li D., Wang L.
PLoS ONE 3:E4053-E4053(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39541 / Ogawa 395 / O395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000626 Genomic DNA. Translation: ABQ19258.1.
CP001236 Genomic DNA. Translation: ACP11031.1.
RefSeqYP_001215916.1. NC_009456.1.
YP_002821267.1. NC_012583.1.

3D structure databases

ProteinModelPortalA5EYL9.
SMRA5EYL9. Positions 3-338.
ModBaseSearch...

Protein-protein interaction databases

STRING345073.VC0395_1080.

Proteomic databases

PRIDEA5EYL9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ19258; ABQ19258; VC0395_1080.
ACP11031; ACP11031; VC395_A0188.
GeneID5134395.
7777261.
KEGGvco:VC0395_1080.
vcr:VC395_A0188.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0516.
HOGENOMHOG000165756.
KOK00364.
OMACSCAGDV.
ProtClustDBPRK05096.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00596. GMP_reduct_type1.
InterProIPR013785. Aldolase_TIM.
IPR005993. GMP_reduct1.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PfamPF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFPIRSF000235. GMP_reductase. 1 hit.
TIGRFAMsTIGR01305. GMP_reduct_1. 1 hit.
PROSITEPS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUAC_VIBC3
AccessionPrimary (citable) accession number: A5EYL9
Secondary accession number(s): C3M7N5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: June 12, 2007
Last modified: May 1, 2013
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families