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C2DMY0 (C2DMY0_ECOLX) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 15. 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:
GMP reductase HAMAP MF_00596 RuleBase RU003929

EC=1.7.1.7 HAMAP MF_00596 RuleBase RU003929
Alternative name(s):
Guanosine 5'-monophosphate oxidoreductase HAMAP MF_00596
Gene names
Name:guaC HAMAP MF_00596 EMBL EEJ48596.1
ORF Names:HMPREF0358_1584 EMBL EEJ48596.1
OrganismEscherichia coli 83972 EMBL EEJ48596.1
Taxonomic identifier525281 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

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 MF_00596 RuleBase RU003929

Catalytic activity

Inosine 5'-phosphate + NH3 + NADP+ = guanosine 5'-phosphate + NADPH. SAAS SAAS001093 HAMAP MF_00596 RuleBase RU003929

Subunit structure

Homotetramer By similarity. HAMAP MF_00596

Sequence similarities

Belongs to the IMPDH/GMPR family. RuleBase RU003927

Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily. HAMAP MF_00596

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding108 – 13124NADP By similarity HAMAP MF_00596
Nucleotide binding216 – 23924NADP; ribose moiety By similarity HAMAP MF_00596

Sites

Active site1861Thioimidate intermediate By similarity HAMAP MF_00596
Metal binding1811Potassium; via carbonyl oxygen By similarity HAMAP MF_00596
Metal binding1831Potassium; via carbonyl oxygen By similarity HAMAP MF_00596

Sequences

Sequence LengthMass (Da)Tools
C2DMY0 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: 898F50DA7FD00441

FASTA34737,384
        10         20         30         40         50         60 
MRIEEDLKLG FKDVLIRPKR STLKSRSDVE LERQFTFKHS GQSWSGVPII AANMDTVGTF 

        70         80         90        100        110        120 
SMASALASFD ILTAVHKHYS VEEWQAFINN SSADVLKHVM VSTGTSDADF EKTKQILDLN 

       130        140        150        160        170        180 
PALNFVCIDV ANGYSEHFVQ FVAKAREAWP TKTICAGNVV TGEMCEELIL SGADIVKVGI 

       190        200        210        220        230        240 
GPGSVCTTRV KTGVGYPQLS AVIECADAAH GLGGMIVSDG GCTTPGDVAK AFGGGADFVM 

       250        260        270        280        290        300 
LGGMLAGHEE SGGRIVEENG EKFMLFYGMS SESAMKRHVG GVAEYRAAEG KTVKLPLRGP 

       310        320        330        340 
VENTARDILG GLRSACTYVG ASRLKELTKR TTFIRVQEQE NRIFNNL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
ACGN01000026 Genomic DNA. Translation: EEJ48596.1.

3D structure databases

ProteinModelPortalC2DMY0.
SMRC2DMY0. Positions 9-336.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

PATRIC31219443. VBIEscCol21464_1164.

Family and domain databases

HAMAPMF_00596. GMP_reduct_type1.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR005993. GMP_reduct1.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHERPTHR11911:SF33. PTHR11911:SF33. 1 hit.
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 nameC2DMY0_ECOLX
AccessionPrimary (citable) accession number: C2DMY0
Entry history
Integrated into UniProtKB/TrEMBL: June 16, 2009
Last sequence update: June 16, 2009
Last modified: December 14, 2011
This is version 15 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)