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Database: UniProt/TrEMBL
Entry: G0G624_AMYMS
LinkDB: G0G624_AMYMS
Original site: G0G624_AMYMS 
ID   G0G624_AMYMS            Unreviewed;       451 AA.
AC   G0G624;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   07-JUN-2017, entry version 37.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:AEK39706.1};
GN   OrderedLocusNames=RAM_06070 {ECO:0000313|EMBL:AEK39706.1};
OS   Amycolatopsis mediterranei (strain S699) (Nocardia mediterranei).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Amycolatopsis.
OX   NCBI_TaxID=713604 {ECO:0000313|EMBL:AEK39706.1, ECO:0000313|Proteomes:UP000006138};
RN   [1] {ECO:0000313|EMBL:AEK39706.1, ECO:0000313|Proteomes:UP000006138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S699 {ECO:0000313|EMBL:AEK39706.1,
RC   ECO:0000313|Proteomes:UP000006138};
RX   PubMed=21914879; DOI=10.1128/JB.05819-11;
RA   Verma M., Kaur J., Kumar M., Kumari K., Saxena A., Anand S., Nigam A.,
RA   Ravi V., Raghuvanshi S., Khurana P., Tyagi A.K., Khurana J.P., Lal R.;
RT   "Whole genome sequence of the rifamycin B-producing strain
RT   Amycolatopsis mediterranei S699.";
RL   J. Bacteriol. 193:5562-5563(2011).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP002896; AEK39706.1; -; Genomic_DNA.
DR   RefSeq; WP_013223100.1; NC_018266.1.
DR   ProteinModelPortal; G0G624; -.
DR   EnsemblBacteria; AEK39706; AEK39706; RAM_06070.
DR   KEGG; amm:AMES_1189; -.
DR   KEGG; amn:RAM_06070; -.
DR   PATRIC; fig|713604.12.peg.1245; -.
DR   KO; K07250; -.
DR   OMA; RVGNYLT; -.
DR   OrthoDB; POG091H0APS; -.
DR   Proteomes; UP000006138; Chromosome.
DR   GO; GO:0003867; F:4-aminobutyrate transaminase activity; IEA:InterPro.
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; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   InterPro; IPR004632; 4NH2But_aminotransferase_bac.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
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:AEK39706.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006138};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006138};
KW   Transferase {ECO:0000313|EMBL:AEK39706.1}.
SQ   SEQUENCE   451 AA;  46770 MW;  6F245C579293890B CRC64;
     MTASTTAGPQ APAPRQRRLQ TEIPGPLSRE LQQRRAAAVA AGVSSVLPVY VTSASGGLLT
     DADGNVLIDF GSGIAVTNVG HSAPAVVDRV RKQACWFTHT CFMVTPYEGY VEVCEALAEL
     TPGDHAKKSV LFNSGAEAVE NAVKIARVAT GRQAVVVFDH AYHGRTNLTM GMTAKSVPYK
     HGFGPFAPEL YRVPGSYPFR DGLSGPEAAA LAIDRIEKQI GGDQVAAVVL EPIQGEGGFI
     EPARGFLPAI AAWCRENGVV YVADEVQTGF CRTGSWFAST DEDVVPDLIA TAKGIAGGLP
     LSAVTGRAAL LDAVGPGGLG GTYGGNPIAC AAALGSIETM KTEHLAASAK RIEGVVLPRL
     RALASETGVI GDVRGRGAML AAEFVKPGSA EPDADLTKRV AAACHRAGVV VLTCGTYGNV
     VRLLPPLSLA DDLLDEGLSV LEHAVRTEVR A
//
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