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 P60560


[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_ECOLI
Primary accession number P60560
Secondary accession numbers P15344 P78048
Integrated into Swiss-Prot on March 15, 2004
Sequence was last modified on March 15, 2004 (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: b0104, JW0101
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=2904262 [NCBI, ExPASy, EBI, Israel, Japan]
Andrews S.C., Guest J.R.;
"Nucleotide sequence of the gene encoding the GMP reductase of Escherichia coli K12.";
Biochem. J. 255:35-43(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/nar/22.9.1637; PubMed=8202364 [NCBI, ExPASy, EBI, Israel, Japan]
Fujita N., Mori H., Yura T., Ishihama A.;
"Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region.";
Nucleic Acids Res. 22:1637-1639(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO 233-235.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 244-347.
STRAIN=K12;
DOI=10.1016/0378-1119(94)90851-6; PubMed=7959070 [NCBI, ExPASy, EBI, Israel, Japan]
Whitchurch C.B., Mattick J.S.;
"Escherichia coli contains a set of genes homologous to those involved in protein secretion, DNA uptake and the assembly of type-4 fimbriae in other bacteria.";
Gene 150:9-15(1994).
[6]
PROTEIN SEQUENCE OF 1-12.
STRAIN=K12 / EMG2;
PubMed=9298646 [NCBI, ExPASy, EBI, Israel, Japan]
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
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
X07917; CAA30751.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73215.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAB96673.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L28105; AAC36926.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR H64732; H64732.
RefSeq AP_000766.1; -.
NP_414646.1; -.
3D structure databases
HSSP P12268; 1B3O. [HSSP ENTRY / PDB]
ModBase P60560.
Protein-protein interaction databases
IntAct P60560; -.
Enzyme and pathway databases
BioCyc EcoCyc:GMP-REDUCT-MON; -.
MetaCyc:GMP-REDUCT-MON; -.
2D gel databases
ECO2DBASE H037.4; 6TH EDITION.
Organism-specific databases
EchoBASE EB0417; -.
EcoGene EG10422; guaC.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
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 P60560.
Genome annotation databases
GeneID 948986; -.
GenomeReviews U00096_GR; b0104.
AP009048_GR; JW0101.
KEGG ecj:JW0101; -.
eco:b0104; -.
Phylogenomic databases
HOGENOM P60560; -.
Genome annotation databases
CMR P60560; b0104.
Other
ProtoNet P60560.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; Metal-binding; NADP; Oxidoreductase; Potassium.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   347  347     GMP reductase. PRO_0000093735
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). 
CONFLICT   233   235        GGG -> AR (in Ref. 1 and 2). 
Sequence information
Length: 347 AA [This is the length of the unprocessed precursor] Molecular weight: 37384 Da [This is the MW of the unprocessed precursor] CRC64: 898F50DA7FD00441 [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 GLGGMIVSDG GCTTPGDVAK AFGGGADFVM 

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

       310        320        330        340 
VENTARDILG GLRSACTYVG ASRLKELTKR TTFIRVQEQE NRIFNNL 

P60560 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!