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Database: UniProt/TrEMBL
Entry: A9HXB9_BORPD
LinkDB: A9HXB9_BORPD
Original site: A9HXB9_BORPD 
ID   A9HXB9_BORPD            Unreviewed;       421 AA.
AC   A9HXB9;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   28-MAR-2018, entry version 58.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:CAP43746.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:CAP43746.1};
GN   Name=goaG2 {ECO:0000313|EMBL:CAP43746.1};
GN   OrderedLocusNames=Bpet3403 {ECO:0000313|EMBL:CAP43746.1};
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100 {ECO:0000313|Proteomes:UP000001225};
RN   [1] {ECO:0000313|EMBL:CAP43746.1, ECO:0000313|Proteomes:UP000001225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448
RC   {ECO:0000313|Proteomes:UP000001225};
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A.,
RA   Pieper D.H., Koebnik R., Lechner M., Bartels D., Buhrmester J.,
RA   Choudhuri J.V., Ebensen T., Gaigalat L., Herrmann S., Khachane A.N.,
RA   Larisch C., Link S., Linke B., Meyer F., Mormann S., Nakunst D.,
RA   Rueckert C., Schneiker-Bekel S., Schulze K., Vorhoelter F.J.,
RA   Yevsa T., Engle J.T., Goldman W.E., Puehler A., Goebel U.B.,
RA   Goesmann A., Bloecker H., Kaiser O., Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the
RT   metabolic versatility of environmental bacteria and virulence traits
RT   of pathogenic Bordetellae.";
RL   BMC Genomics 9:449-449(2008).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; AM902716; CAP43746.1; -; Genomic_DNA.
DR   ProteinModelPortal; A9HXB9; -.
DR   STRING; 340100.Bpet3403; -.
DR   EnsemblBacteria; CAP43746; CAP43746; Bpet3403.
DR   KEGG; bpt:Bpet3403; -.
DR   eggNOG; ENOG4108JPW; Bacteria.
DR   eggNOG; COG0160; LUCA.
DR   HOGENOM; HOG000020206; -.
DR   KO; K00823; -.
DR   OMA; VMCGFYA; -.
DR   OrthoDB; POG091H0APS; -.
DR   Proteomes; UP000001225; 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:CAP43746.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001225};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001225};
KW   Transferase {ECO:0000313|EMBL:CAP43746.1}.
SQ   SEQUENCE   421 AA;  44823 MW;  82B777353E7703DC CRC64;
     MQNRDLNTRR SLATPRGVGV MCDLYAVRAE NATLWDSTGK EYIDFAGGIA VLNTGHRHPK
     VKAAVAEQLE AFTHTAYQIV PYESYVALAE RINALAPIDG LKKTAFFTTG VEAVENAVKI
     ARAYTGRSGV VAFTGSFHGR TMLGMALTGK VAPYKLAFGP MPGDIYHVPF PNGTQDISVA
     DSLKALDLLF KSDIDPQRVA AIIIEPVQGE GGFNITPPEL MTALRKVCDE HGIMLIADEV
     QTGFARTGKL FAMQHHGVQA DLITMAKSLG GGFPISGVVG RAEVMDGPAP GGLGGTYAGN
     PLAVAAAHAV LDVIEEEQLC ARAEQLGRRL QDHLNKLRPR CPAIADVRGL GSMVALELND
     PATGKPDAAA VKRVQDEAIQ RGLILLSCGV YGNVLRFLYP LTIPDAQFAQ ALDILADVLT
     A
//
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