GenomeNet

Database: UniProt/TrEMBL
Entry: A0A0H3D0G9_AMYMU
LinkDB: A0A0H3D0G9_AMYMU
Original site: A0A0H3D0G9_AMYMU 
ID   A0A0H3D0G9_AMYMU        Unreviewed;       451 AA.
AC   A0A0H3D0G9;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   05-JUL-2017, entry version 11.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:ADJ43011.1};
GN   Name=gabT {ECO:0000313|EMBL:ADJ43011.1};
GN   OrderedLocusNames=AMED_1196 {ECO:0000313|EMBL:ADJ43011.1};
OS   Amycolatopsis mediterranei (strain U-32).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Amycolatopsis.
OX   NCBI_TaxID=749927 {ECO:0000313|EMBL:ADJ43011.1, ECO:0000313|Proteomes:UP000000328};
RN   [1] {ECO:0000313|EMBL:ADJ43011.1, ECO:0000313|Proteomes:UP000000328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U-32 {ECO:0000313|Proteomes:UP000000328};
RX   PubMed=20567260; DOI=10.1038/cr.2010.87;
RA   Zhao W., Zhong Y., Yuan H., Wang J., Zheng H., Wang Y., Cen X., Xu F.,
RA   Bai J., Han X., Lu G., Zhu Y., Shao Z., Yan H., Li C., Peng N.,
RA   Zhang Z., Zhang Y., Lin W., Fan Y., Qin Z., Hu Y., Zhu B., Wang S.,
RA   Ding X., Zhao G.P.;
RT   "Complete genome sequence of the rifamycin SV-producing Amycolatopsis
RT   mediterranei U32 revealed its genetic characteristics in phylogeny and
RT   metabolism.";
RL   Cell Res. 20:1096-1108(2010).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP002000; ADJ43011.1; -; Genomic_DNA.
DR   RefSeq; WP_013223100.1; NC_014318.1.
DR   RefSeq; YP_003763413.1; NC_014318.1.
DR   ProteinModelPortal; A0A0H3D0G9; -.
DR   STRING; 749927.AMED_1196; -.
DR   EnsemblBacteria; ADJ43011; ADJ43011; AMED_1196.
DR   GeneID; 9435409; -.
DR   KEGG; amd:AMED_1196; -.
DR   PATRIC; fig|749927.5.peg.1227; -.
DR   KO; K07250; -.
DR   OMA; RVGNYLT; -.
DR   Proteomes; UP000000328; 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:ADJ43011.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000328};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Transferase {ECO:0000313|EMBL:ADJ43011.1}.
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
//
DBGET integrated database retrieval system