ID   B2JSD7_PARP8            Unreviewed;       430 AA.
AC   B2JSD7;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:ACC73957.1};
GN   OrderedLocusNames=Bphy_4851 {ECO:0000313|EMBL:ACC73957.1};
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC73957.1, ECO:0000313|Proteomes:UP000001192};
RN   [1] {ECO:0000313|Proteomes:UP000001192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC   {ECO:0000313|Proteomes:UP000001192};
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA   James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA   Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA   Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT   range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(2014).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001044; ACC73957.1; -; Genomic_DNA.
DR   RefSeq; WP_012404126.1; NZ_CADFGH010000014.1.
DR   AlphaFoldDB; B2JSD7; -.
DR   STRING; 391038.Bphy_4851; -.
DR   KEGG; bph:Bphy_4851; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_4; -.
DR   OrthoDB; 3398487at2; -.
DR   Proteomes; UP000001192; Chromosome 2.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004632; 4NH2But_aminotransferase_bac.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR00700; GABAtrnsam; 1.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000313|EMBL:ACC73957.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001192};
KW   Transferase {ECO:0000313|EMBL:ACC73957.1}.
SQ   SEQUENCE   430 AA;  46254 MW;  37C3569B7190A2AC CRC64;
     MSDTNADLLD RKNAATPRGV GVMCEFYAAR AENAELWDVE GRRFIDFAAG IAVCNTGHRH
     PKIVAAIREQ LDFFTHTAYQ IVPYASYVTL AEKINERAPG NYPKKTAFFT TGAEAVENAI
     KIARAATGRS GVIAFTGGFH GRTMMGMALT GKVAPYKLNF GPFPAEVFHA PFPNPLHGVT
     TTDSLKAIEH LFKADIEPKR VAAIIFEPVQ GEGGFHPAPA EFVRALRKLC DEHGILLIAD
     EVQTGFARTG KLFAMQHYDV VPDLMTMAKS LAGGMPLSGV VGRAELMDAA APGGLGGTYA
     GNPLAIAAAH AVLDIIDEEA LCDRATQLGD RIKANLKNLR EIVPQIADIR GPGAMVAVEF
     CKPGSEHEPD PTFTKQVQAK ALERGLLLLV CGTYANVIRF LFPLTVEENV FDEALSILQD
     VLKETAAVPA
//