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Database: UniProt/TrEMBL
Entry: Q0B6G2_BURCM
LinkDB: Q0B6G2_BURCM
Original site: Q0B6G2_BURCM 
ID   Q0B6G2_BURCM            Unreviewed;       446 AA.
AC   Q0B6G2;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   25-OCT-2017, entry version 70.
DE   SubName: Full=4-aminobutyrate aminotransferase apoenzyme {ECO:0000313|EMBL:ABI90261.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:ABI90261.1};
GN   OrderedLocusNames=Bamb_4711 {ECO:0000313|EMBL:ABI90261.1};
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia
OS   cepacia (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670 {ECO:0000313|EMBL:ABI90261.1, ECO:0000313|Proteomes:UP000000662};
RN   [1] {ECO:0000313|Proteomes:UP000000662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD {ECO:0000313|Proteomes:UP000000662};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T.,
RA   Konstantinidis K., Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP000441; ABI90261.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q0B6G2; -.
DR   STRING; 339670.Bamb_4711; -.
DR   EnsemblBacteria; ABI90261; ABI90261; Bamb_4711.
DR   KEGG; bam:Bamb_4711; -.
DR   eggNOG; ENOG4108JPW; Bacteria.
DR   eggNOG; COG0160; LUCA.
DR   HOGENOM; HOG000020206; -.
DR   KO; K00823; -.
DR   OMA; ICWRAFE; -.
DR   OrthoDB; POG091H0APS; -.
DR   Proteomes; UP000000662; Chromosome 2.
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; 3.40.640.10; -; 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:ABI90261.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000662};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Transferase {ECO:0000313|EMBL:ABI90261.1}.
SQ   SEQUENCE   446 AA;  47734 MW;  1FED7E93AD06B8D0 CRC64;
     MGCQRGRFLS HRTDIKEMTV KNADLQARKN AATPRGVGVM CDFYAARAEN AELWDVEGRR
     FIDFAAGIAV LNTGHRHPKI VKAITEQLNS FTHTAYQIVP YASYVELAEK INGRAPGDFP
     KKTAFFTTGA EAVENAIKIA RAATGRPGVI AFSGGFHGRT MMGMALTGKV APYKLNFGPF
     PGDVFHAPYP NALHGVSTAD SIKAIEMLFK ADIDPKRVAA IIFEPVQGEG GFYPAPAEFV
     RALRKICNEH GILLIADEVQ TGFARTGKLF AMQHYDVLAD LITMAKSLAG GMPLSGVVGR
     ADVMDAAAPG GLGGTYAGNP LAVASAHAVL EIIDEEKLCE RATQLGDVLK AKLNSLQADV
     PQIADVRGPG AMVAVEFLKP GSGEPDADFT KRVQARALER GLLLLVCGVY SNVVRFLFPL
     TIPQAVFDEA LVILEEVLKE TVGVPA
//
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