GenomeNet

Database: UniProt/TrEMBL
Entry: K0MC26_BORPB
LinkDB: K0MC26_BORPB
Original site: K0MC26_BORPB 
ID   K0MC26_BORPB            Unreviewed;       421 AA.
AC   K0MC26;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   28-FEB-2018, entry version 20.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:CCJ48843.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:CCJ48843.1};
GN   Name=goaG {ECO:0000313|EMBL:CCJ48843.1};
GN   OrderedLocusNames=BN117_1510 {ECO:0000313|EMBL:CCJ48843.1};
OS   Bordetella parapertussis (strain Bpp5).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1208660 {ECO:0000313|EMBL:CCJ48843.1, ECO:0000313|Proteomes:UP000008035};
RN   [1] {ECO:0000313|EMBL:CCJ48843.1, ECO:0000313|Proteomes:UP000008035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bpp5 {ECO:0000313|EMBL:CCJ48843.1,
RC   ECO:0000313|Proteomes:UP000008035};
RX   PubMed=23051057; DOI=10.1186/1471-2164-13-545;
RA   Park J., Zhang Y., Buboltz A.M., Zhang X., Schuster S.C., Ahuja U.,
RA   Liu M., Miller J.F., Sebaihia M., Bentley S.D., Parkhill J.,
RA   Harvill E.T.;
RT   "Comparative genomics of the classical Bordetella subspecies: the
RT   evolution and exchange of virulence-associated diversity amongst
RT   closely related pathogens.";
RL   BMC Genomics 13:545-545(2012).
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 https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; HE965803; CCJ48843.1; -; Genomic_DNA.
DR   RefSeq; WP_015039384.1; NC_018828.1.
DR   RefSeq; YP_006895483.1; NC_018828.1.
DR   ProteinModelPortal; K0MC26; -.
DR   EnsemblBacteria; CCJ48843; CCJ48843; BN117_1510.
DR   GeneID; 13889546; -.
DR   KEGG; bpar:BN117_1510; -.
DR   KO; K00823; -.
DR   BioCyc; BPAR1208660:G1HD3-1527-MONOMER; -.
DR   Proteomes; UP000008035; Chromosome.
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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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:CCJ48843.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008035};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Transferase {ECO:0000313|EMBL:CCJ48843.1}.
SQ   SEQUENCE   421 AA;  44823 MW;  1673E5001020951A CRC64;
     MKNRDLNTRR TLATPRSVGV MCDFYAVRAE NSTLWDAEGK EYIDFAGGIA VLNTGHRHPK
     VKAAIAAQLD NFTHTAYQIV PYEGYVSLAE RINAVAPIEG LKKTAFFTTG VEAVENAVKI
     ARAYTGRSGV VTFSGAFHGR TMMGMALTGK VAPYKLAFGP MPGDVFHVPF PNATQAISVA
     DSLKALDLLF KVDIDPKRVA AIIIEPVQGE GGFNVTPPEL MQALRKVCDE HGILLIADEV
     QTGFARTGKL FAMQHHSVQA DLITMAKSLG GGMPISGVVG RAEVMDGPAA GGLGGTYAGN
     PLAVAAAHAV LDVIAEEKLC ERAAELGKRL MDRLEGLRAK CPAIADVRGL GSMVALELND
     PATGKPDAEA VKRIQQQAIE RGLILLSCGV YGNVLRFLYP LTIPDDQFAR ALDILAETIA
     A
//
DBGET integrated database retrieval system