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UniProtKB/Swiss-Prot entry Q5PDH8

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

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Entry information
Entry name GUAC_SALPA
Primary accession number Q5PDH8
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on January 4, 2005 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 33)
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: SPA0145
From
Salmonella paratyphi A [TaxID: 54388] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Salmonella.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 9150 / SARB42;
DOI=10.1038/ng1470; PubMed=15531882 [NCBI, ExPASy, EBI, Israel, Japan]
McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F., Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L., Spieth J., Wilson R.K.;
"Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid.";
Nat. Genet. 36:1268-1274(2004).
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
CP000026; AAV76178.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_149490.1; -.
3D structure databases
ModBase Q5PDH8.
Enzyme and pathway databases
BioCyc SENT295319:SPA0145-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 Q5PDH8.
Genome annotation databases
GeneID 3177417; -.
GenomeReviews CP000026_GR; SPA0145.
KEGG spt:SPA0145; -.
Phylogenomic databases
HOGENOM Q5PDH8; -.
Genome annotation databases
CMR Q5PDH8; SPA0145.
Other
ProtoNet Q5PDH8.
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_1000025617
NP_BIND   108   131  24     NADP (By similarity). 
NP_BIND   216   239  24     NADP; ribose moiety (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: 37139 Da [This is the MW of the unprocessed precursor] CRC64: 71223D342F001B45 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MRIEEDLKLG FKDVLIRPKR STLKSRSDVE LERQFTFKHS GQTWSGVPII AANMDTVGTF 

        70         80         90        100        110        120 
EMAQALAGFD ILTAVHKHYT VEEWAAFINT ASADVLKHVM VSTGTSDADF EKTVQILALN 

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

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

       250        260        270        280        290        300 
LGGMLAGHEE SGGSVVEENG EKFMLFYGMS SESAMNRHVG GVAKYRAAEG KTVKLPLRGP 

       310        320        330        340 
VGNTARDILG GLRSACTYVG ASRLKELTKR TTFIRVQEQE NRIFNSL
Q5PDH8 in FASTA format

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