(data stored in ACNUC7421 zone)

SWISSPROT: C6B0E6_RHILS

ID   C6B0E6_RHILS            Unreviewed;       388 AA.
AC   C6B0E6;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 48.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   OrderedLocusNames=Rleg_0254 {ECO:0000313|EMBL:ACS54565.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54565.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54565.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54565.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU000481};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU000481}.
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DR   EMBL; CP001622; ACS54565.1; -; Genomic_DNA.
DR   RefSeq; WP_012755978.1; NC_012850.1.
DR   ProteinModelPortal; C6B0E6; -.
DR   EnsemblBacteria; ACS54565; ACS54565; Rleg_0254.
DR   KEGG; rlg:Rleg_0254; -.
DR   HOGENOM; HOG000223062; -.
DR   OMA; GWLRWCF; -.
DR   OrthoDB; POG091H00QO; -.
DR   BioCyc; RLEG395491:GHX2-257-MONOMER; -.
DR   Proteomes; UP000002256; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6B0E6.
DR   SWISS-2DPAGE; C6B0E6.
KW   Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW   ECO:0000313|EMBL:ACS54565.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Transferase {ECO:0000256|RuleBase:RU000481,
KW   ECO:0000313|EMBL:ACS54565.1}.
FT   DOMAIN       40    381       Aminotran_1_2. {ECO:0000259|Pfam:
FT                                PF00155}.
SQ   SEQUENCE   388 AA;  42119 MW;  AE391975A3E93333 CRC64;
     MSIVSSLSPR ALAAPESGIV ELVNYARGRE GLLPLWVGEG DLPTPDFISR AAMDALASGE
     TFYTWQRGIP ELRQALSDYY DRHFGIRLPV EHFYVTGSGM QAIQIAVQAL TSPGDELVYL
     SPSWPNIAAA LEIAGARSLS VELQFEGGKW AVDLDRIETA ITPKTKGIFI NTPSNPTGWT
     ATKQDLGDLL ALARKHDLWI MADEIYARYY FAGGRAPSFL DVMEPDDKII FVNSFSKNWS
     MTGWRVGWIV APPEMGQVLE NLIQYSTSGV AQFMQKGAVA ALDQGDDFVA ANIAKAARSR
     DTLCDALVAT NRVETLKPDG AIYAFLKIDG VADSRTAALD IVDKTGVGLA PGTAFGSGGE
     LFLRACFLRD PTQVAIAAER LCDYILKL
//

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