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UniProtKB/Swiss-Prot entry Q8K9U0

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

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Entry information
Entry name GUAC_BUCAP
Primary accession number Q8K9U0
Secondary accession numbers None
Integrated into Swiss-Prot on November 8, 2002
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 4, 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: BUsg_198
From
Buchnera aphidicola subsp. Schizaphis graminum [TaxID: 98794] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1071278; PubMed=12089438 [NCBI, ExPASy, EBI, Israel, Japan]
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
"50 million years of genomic stasis in endosymbiotic bacteria.";
Science 296:2376-2379(2002).
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
AE013218; AAM67762.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_660551.1; -.
3D structure databases
HSSP P12268; 1B3O. [HSSP ENTRY / PDB]
ModBase Q8K9U0.
Enzyme and pathway databases
BioCyc BAPH198804:BUSG198-MON; -.
Ontologies
GO
GO:0003920; Molecular function: GMP reductase activity (inferred from electronic annotation from HAMAP).
GO:0030955; Molecular function: potassium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.
ProtoNet Q8K9U0.
Genome annotation databases
GeneID 1005395; -.
GenomeReviews AE013218_GR; BUsg_198.
KEGG bas:BUsg198; -.
Phylogenomic databases
HOGENOM Q8K9U0; -.
Genome annotation databases
CMR Q8K9U0; BUsg_198.
Other
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   349  349     GMP reductase. PRO_0000093733
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: 349 AA [This is the length of the unprocessed precursor] Molecular weight: 38618 Da [This is the MW of the unprocessed precursor] CRC64: D5CCF618376665CF [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MRIEEDIKLG FKDVLIRPKR STLKSRSEVN LIRCFSFKYS TMKWFGIPLI AANMDTIGTF 

        70         80         90        100        110        120 
RMAEALSKFN ILTAVHKYYS FDEWKNFISV SSKEILEHVI VSIGTSNLDF FKIKKIFSLS 

       130        140        150        160        170        180 
SELKYICIDV ANGYSEHFVS FLKKIRSFFP DKIICAGNVV TGEMVEELIL SGADIVKVGI 

       190        200        210        220        230        240 
GPGSVCTTRL KTGIGYPQLS AIIECADAAH GLNGQIISDG GCTVSGDIAK AFGGGADFVM 

       250        260        270        280        290        300 
LGGMFAGHTE CLGEIIQEKS KKFMLFYGMS STSAMKRYTG KIPGYRASEG KIVKIPFRGN 

       310        320        330        340 
VDVTVRDILG GLRSSCTYVG AQKLKELTKR TTFIRVSEQE NCIFNNFKN
Q8K9U0 in FASTA format

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