ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q8X984

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name GUAC_ECO57
Primary accession number Q8X984
Secondary accession numbers None
Integrated into Swiss-Prot on November 8, 2002
Sequence was last modified on March 1, 2002 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 47)
Name and origin of the protein
Protein name GMP reductase
Synonyms EC 1.7.1.7
Guanosine 5'-monophosphate oxidoreductase
Guanosine monophosphate reductase
Gene name
Name: guaC
OrderedLocusNames: Z0114, ECs0108
From
Escherichia coli O157:H7 [TaxID: 83334] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
DOI=10.1038/35054089; PubMed=11206551 [NCBI, ExPASy, EBI, Israel, Japan]
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.;
"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
Nature 409:529-533(2001).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
DOI=10.1093/dnares/8.1.11; PubMed=11258796 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S., Shiba T., Hattori M., Shinagawa H.;
"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12.";
DNA Res. 8:11-22(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE005174; AAG54408.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000007; BAB33531.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D85493; D85493.
D90642; D90642.
RefSeq NP_285800.1; -.
NP_308135.1; -.
3D structure databases
HSSP P12268; 1B3O. [HSSP ENTRY / PDB]
ModBase Q8X984.
Enzyme and pathway databases
BioCyc ECOL83334:ECS0108-MON; -.
Ontologies
GO
GO:0003920; Molecular function: GMP reductase activity (inferred from electronic annotation from HAMAP).
GO:0006163; Biological process: purine nucleotide metabolic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00596; -; 1.
PBIL [Tree]
InterPro IPR013785; Aldolase_TIM.
IPR005993; GMP_reduct1.
IPR015875; IMP_DH/GMP_Rdtase_CS.
IPR001093; IMP_DHase_GMPRtase.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 1.
Pfam PF00478; IMPDH; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000235; GMP_reductase; 1.
TIGRFAMs TIGR01305; GMP_reduct_1; 1.
PROSITE PS00487; IMP_DH_GMP_RED; 1.
BLOCKS Q8X984.
Genome annotation databases
GeneID 913617; -.
956795; -.
GenomeReviews BA000007_GR; ECs0108.
AE005174_GR; Z0114.
KEGG ece:Z0114; -.
ecs:ECs0108; -.
Phylogenomic databases
HOGENOM Q8X984; -.
Genome annotation databases
CMR Q8X984; Z0114.
Other
ProtoNet Q8X984.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Metal-binding; NADP; Oxidoreductase; Potassium.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   347  347     GMP reductase. PRO_0000093737
NP_BIND   108   131  24     NADP (By similarity). 
NP_BIND   216   239  24     NADP (By similarity). 
ACT_SITE   186   186        Thioimidate intermediate (By similarity). 
METAL   181   181        Potassium; via carbonyl oxygen (By similarity). 
METAL   183   183        Potassium; via carbonyl oxygen (By similarity). 
Sequence information
Length: 347 AA [This is the length of the unprocessed precursor] Molecular weight: 37398 Da [This is the MW of the unprocessed precursor] CRC64: 912C5AE96D400441 [This is a checksum on the sequence] 
        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 GLGGMIISDG GCTTPGDVAK AFGGGADFVM 

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

       310        320        330        340 
VENTARDILG GLRSACTYVG ASRLKELTKR TTFIRVQEQE NRIFNNL
Q8X984 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by kr flag YPRC Korea Mirror sites: Australia Brazil Canada China Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!