ID   D3P3U2_AZOS1            Unreviewed;       429 AA.
AC   D3P3U2;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:BAI75321.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:BAI75321.1};
GN   Name=gabT {ECO:0000313|EMBL:BAI75321.1};
GN   OrderedLocusNames=AZL_c00280 {ECO:0000313|EMBL:BAI75321.1};
OS   Azospirillum sp. (strain B510).
OG   Plasmid pAB510c {ECO:0000313|EMBL:BAI75321.1,
OG   ECO:0000313|Proteomes:UP000002040}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=137722 {ECO:0000313|EMBL:BAI75321.1, ECO:0000313|Proteomes:UP000002040};
RN   [1] {ECO:0000313|EMBL:BAI75321.1, ECO:0000313|Proteomes:UP000002040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B510 {ECO:0000313|EMBL:BAI75321.1,
RC   ECO:0000313|Proteomes:UP000002040};
RC   PLASMID=pAB510c {ECO:0000313|EMBL:BAI75321.1};
RX   PubMed=20047946; DOI=10.1093/dnares/dsp026;
RA   Kaneko T., Minamisawa K., Isawa T., Nakatsukasa H., Mitsui H.,
RA   Kawaharada Y., Nakamura Y., Watanabe A., Kawashima K., Ono A., Shimizu Y.,
RA   Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M., Nakazaki N.,
RA   Nakayama S., Yamada M., Tabata S., Sato S.;
RT   "Complete genomic structure of the cultivated rice endophyte Azospirillum
RT   sp. B510.";
RL   DNA Res. 17:37-50(2010).
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}.
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DR   EMBL; AP010949; BAI75321.1; -; Genomic_DNA.
DR   RefSeq; WP_012977153.1; NC_013857.1.
DR   AlphaFoldDB; D3P3U2; -.
DR   KEGG; azl:AZL_c00280; -.
DR   HOGENOM; CLU_016922_10_0_5; -.
DR   OrthoDB; 9801834at2; -.
DR   Proteomes; UP000002040; Plasmid pAB510c.
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; 3.90.1150.10; 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   PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 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:BAI75321.1}; Plasmid {ECO:0000313|EMBL:BAI75321.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002040};
KW   Transferase {ECO:0000313|EMBL:BAI75321.1}.
SQ   SEQUENCE   429 AA;  45474 MW;  FFF1FC28328A3CF0 CRC64;
     MTTNQSFVAR REAAVSRGIS AGMPVYIDRA ENAEMWDVEG KRFIDFAGGI AVLNTGHRHP
     KVMEAVKAQL DRFTHTCAMV TPYDSFVELA EKLNALVPGR EPKKTAFFTT GAEAVENAVK
     VARAATGRPG VVAFSGGFHG RTLLTMGLTG KVVPYKVGFG PFPAEIFHVP FPNAYRGISE
     AESLKALENL FKSDVDPARV AAIIIEPVQG EGGFNIASPS FLQALRAVCD KHGIVMIVDE
     IQTGFARTGK MFAVEHAGIE PDLVTMAKSL AGGFPLSAVT GKAALMDAPI PGGLGGTYAG
     SPLATTAALA VINVIEEEKL VERSEKLGEH IAGRFRAMAQ RNSLSVIGDV RNLGAMVAME
     LVTDRETKEP AADLTKALVA KAAEKGLVLL SCGTYANVIR ILVPLTASDA LVDEGLDIIE
     RSLEELVSA
//