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UniProtKB/Swiss-Prot entry Q89AV2

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

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Entry information
Entry name DYR_BUCBP
Primary accession number Q89AV2
Secondary accession numbers None
Integrated into Swiss-Prot on November 14, 2003
Sequence was last modified on June 1, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 37)
Name and origin of the protein
Protein name Dihydrofolate reductase
Synonym EC 1.5.1.3
Gene name
Name: folA
OrderedLocusNames: bbp_133
From
Buchnera aphidicola subsp. Baizongia pistaciae [TaxID: 135842] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0235981100; PubMed=12522265 [NCBI, ExPASy, EBI, Israel, Japan]
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
"Reductive genome evolution in Buchnera aphidicola.";
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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
AE016826; AAO26867.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_777762.1; -.
3D structure databases
HSSP P00379; 1DHI. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
ModBase Q89AV2.
Enzyme and pathway databases
BioCyc BAPH224915:BBP_133-MON; -.
Ontologies
GO
GO:0004146; Molecular function: dihydrofolate reductase activity (inferred from electronic annotation from InterPro).
GO:0050661; Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0006545; Biological process: glycine biosynthetic process (inferred from electronic annotation from InterPro).
GO:0009165; Biological process: nucleotide biosynthetic process (inferred from electronic annotation from InterPro).
GO:0006730; Biological process: one-carbon compound metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR012259; DHFR.
IPR001796; DHFR_reg.
Graphical view of domain structure.
PANTHER PTHR11549:SF1; DHFR; 1.
Pfam PF00186; DHFR_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00070; DHFR.
PROSITE PS00075; DHFR_1; 1.
PS51330; DHFR_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q89AV2.
ProtoNet Q89AV2.
Genome annotation databases
GeneID 1058169; -.
GenomeReviews AE016826_GR; bbp_133.
KEGG bab:bbp133; -.
Phylogenomic databases
HOGENOM Q89AV2; -.
Genome annotation databases
CMR Q89AV2; bbp_133.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; NADP; One-carbon metabolism; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom To Length Description FTId
CHAIN   1   164  164     Dihydrofolate reductase. PRO_0000186385
DOMAIN   2   162  161     DHFR. 
Sequence information
Length: 164 AA [This is the length of the unprocessed precursor] Molecular weight: 19189 Da [This is the MW of the unprocessed precursor] CRC64: DCCF58465EED5949 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MNISIIVAMS QNLVIGQKNS IPWNIPKDLS WFKKHTIKKS IIMGRKTWES IGRVLPMRQN 

        70         80         90        100        110        120 
IVLTRQKNIK NTNVLFVNSI SKAIQSALYK NEIMIIGGSN LYNQMLTSAN KLYITHIEKY 

       130        140        150        160 
ILGDTYFPTY DHLPWKIIFK KKIIEHEKTK NSFYVTFKIL KKIT
Q89AV2 in FASTA format

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