ID   A0A1I4X2Z7_9GAMM        Unreviewed;       448 AA.
AC   A0A1I4X2Z7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:SFN19843.1};
GN   ORFNames=SAMN05216289_10761 {ECO:0000313|EMBL:SFN19843.1};
OS   Dokdonella immobilis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Dokdonella.
OX   NCBI_TaxID=578942 {ECO:0000313|EMBL:SFN19843.1, ECO:0000313|Proteomes:UP000198575};
RN   [1] {ECO:0000313|EMBL:SFN19843.1, ECO:0000313|Proteomes:UP000198575}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.7659 {ECO:0000313|EMBL:SFN19843.1,
RC   ECO:0000313|Proteomes:UP000198575};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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|RuleBase:RU003560}.
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DR   EMBL; FOVF01000007; SFN19843.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4X2Z7; -.
DR   STRING; 578942.SAMN05216289_10761; -.
DR   OrthoDB; 9801052at2; -.
DR   Proteomes; UP000198575; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; 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   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:SFN19843.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198575};
KW   Transferase {ECO:0000313|EMBL:SFN19843.1}.
SQ   SEQUENCE   448 AA;  47659 MW;  54E00AE07C1C2E1F CRC64;
     MKTSHIRTPL PGPRAQALIA RDAEVISPSY PRDYPFAMSH GRGTEVWDVD GNRFLDFAAG
     IAVCATGHAH PRVVEVVRQA AGEFLHISSD YWHEQMVGLG ERLARLAPMR TLAGEAAMSF
     LCQSGTEAVE GAIKLARYVT RRPRFIGFLG GFHGRSMGSL SFTSSKYTQQ LGFAPTMPGV
     THVPYPDPYR PLFAGADQGQ AVLDYIGLLF ERSVPAAEVA AILVEPIQGE GGYIVPPDGF
     LAGLRALCDR HGILLIFDEV QSGVGRTGRM FACEHWGVAP DILTSAKGLG SGLPIGAVVA
     KKSIMAQWKR GAHGNTYGGN PIACAAANAT LDLVEGGFAE NAATVGAHFM DRLGELARRY
     PCIGEVRGRG LMIGLELIGT DGSRKPARAL CDAVITRAFH NGLLLLSCGA STVRFMPPLN
     TSVAEVDEAV ELLDASLEEA LVGSHDPA
//