ID   Q1AS14_RUBXD            Unreviewed;       438 AA.
AC   Q1AS14;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:ABG05814.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:ABG05814.1};
GN   OrderedLocusNames=Rxyl_2903 {ECO:0000313|EMBL:ABG05814.1};
OS   Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1).
OC   Bacteria; Actinomycetota; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC   Rubrobacter.
OX   NCBI_TaxID=266117 {ECO:0000313|EMBL:ABG05814.1, ECO:0000313|Proteomes:UP000006637};
RN   [1] {ECO:0000313|EMBL:ABG05814.1, ECO:0000313|Proteomes:UP000006637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9941 / NBRC 16129 / PRD-1
RC   {ECO:0000313|Proteomes:UP000006637};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA   Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT   "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000386; ABG05814.1; -; Genomic_DNA.
DR   RefSeq; WP_011565823.1; NC_008148.1.
DR   AlphaFoldDB; Q1AS14; -.
DR   STRING; 266117.Rxyl_2903; -.
DR   KEGG; rxy:Rxyl_2903; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_11; -.
DR   OrthoDB; 9801052at2; -.
DR   PhylomeDB; Q1AS14; -.
DR   Proteomes; UP000006637; 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; 3.90.1150.10; 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:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 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:0000313|EMBL:ABG05814.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006637};
KW   Transferase {ECO:0000313|EMBL:ABG05814.1}.
SQ   SEQUENCE   438 AA;  47370 MW;  69CA099177B86753 CRC64;
     MLRAARIRTE IPGPRSRALT ERRRRAISAG LGTALPIWVA EAHGALVTDV DGNTFIDFGG
     GIGVLNAGHT HPRVVEAVRE QVGRLTHACY YVSQYEPYLE LAEKLNELVP GNFEKRSIFV
     NSGAEAVENA IKISRSYTRR PAILAFENAF HGRTMLGMSL TGKADPYRRG FGPFVPEVYR
     VPAPYAYRMP KEESWFDAFR RSLVSVDVSS VAAVIVEPVL GEGGFIPFPP EDLRRLREWC
     TENGAVMVVD EVQTGFGRTG KMFAIEHSGV EPDIVTTAKS LGGGMPIAGV TGRAEIMDSV
     HAGGLGTTYG GNPAACAAAL AVIRAFEEEN LLERSVRVGE RVMEELRAIQ RRHPDFVGDV
     RGLGAMAAME LVTDARSKTP DPARTKGVVE HALQEGLMLL TAGAYGNVIR TLMPLVITDS
     ELEEGLSILS RAVDAAAA
//