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Database: UniProt/TrEMBL
Entry: A4YTI2_BRASO
LinkDB: A4YTI2_BRASO
Original site: A4YTI2_BRASO 
ID   A4YTI2_BRASO            Unreviewed;       433 AA.
AC   A4YTI2;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   25-OCT-2017, entry version 61.
DE   SubName: Full=4-aminobutyrate aminotransferase ((S)-3-amino-2-methylpropionate transaminase) {ECO:0000313|EMBL:CAL77208.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:CAL77208.1};
DE            EC=2.6.1.22 {ECO:0000313|EMBL:CAL77208.1};
GN   Name=gabT {ECO:0000313|EMBL:CAL77208.1};
GN   OrderedLocusNames=BRADO3420 {ECO:0000313|EMBL:CAL77208.1};
OS   Bradyrhizobium sp. (strain ORS 278).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=114615 {ECO:0000313|EMBL:CAL77208.1, ECO:0000313|Proteomes:UP000001994};
RN   [1] {ECO:0000313|EMBL:CAL77208.1, ECO:0000313|Proteomes:UP000001994}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ORS 278 {ECO:0000313|Proteomes:UP000001994};
RX   PubMed=17540897; DOI=10.1126/science.1139548;
RA   Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.C.,
RA   Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA   Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S.,
RA   Rouy Z., Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.S.,
RA   Saunders E., Bruce D., Richardson P., Normand P., Dreyfus B.,
RA   Pignol D., Stacey G., Emerich D., Vermeglio A., Medigue C.,
RA   Sadowsky M.;
RT   "Legumes symbioses: absence of nod genes in photosynthetic
RT   bradyrhizobia.";
RL   Science 316:1307-1312(2007).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CU234118; CAL77208.1; -; Genomic_DNA.
DR   ProteinModelPortal; A4YTI2; -.
DR   STRING; 114615.BRADO3420; -.
DR   EnsemblBacteria; CAL77208; CAL77208; BRADO3420.
DR   KEGG; bra:BRADO3420; -.
DR   eggNOG; ENOG4108JPW; Bacteria.
DR   eggNOG; COG0160; LUCA.
DR   HOGENOM; HOG000020206; -.
DR   KO; K07250; -.
DR   OMA; APYESYV; -.
DR   OrthoDB; POG091H0APS; -.
DR   Proteomes; UP000001994; Chromosome.
DR   GO; GO:0047298; F:(S)-3-amino-2-methylpropionate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IEA:InterPro.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.90.1150.10; -; 3.
DR   InterPro; IPR004632; 4NH2But_aminotransferase_bac.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00700; GABAtrnsam; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:CAL77208.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001994};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001994};
KW   Transferase {ECO:0000313|EMBL:CAL77208.1}.
SQ   SEQUENCE   433 AA;  45917 MW;  F9270C088EA87AE2 CRC64;
     MAVDQAVNPA ANQQLLARRH EAVVRGVSYA TPLFADRALN SEVWDVEGKR YVDFAGGIAV
     LNTGHCHPHV VAAIRAQLDR FTHTCFQVLQ YEPYVRLSER LNALAPVAGP AKSILLTTGA
     EATENAIKIA RAATGRSGII AFTGAFHGRT ALANAMTGKV MPYKRPFGPP LPGIWHAPFP
     VAGSNVSVED TLSYINFIFK ADIDASQVAA IIIEPVQGEG GFHQAPPDLM RGLRRICDAN
     GIVLIADEVQ TGFGRTGKMF AMEHYDVQPD LICVAKSLAG GMPLSGVIGR SAIMDAAEPG
     GLGGTYGGNP LACAAALAVL DVFEQEKLVE RANTIGDRLR AAITRFSRAN NLVPVSGPRG
     PGAMVAFDIL KQRGSDEPDP EMTKRVTRVA HENGLILLSC GVTASTIRIL VPLTASNEIV
     DEGLAILEKC LAA
//
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