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
//
