ID Q6F767_ACIAD Unreviewed; 428 AA.
AC Q6F767;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE SubName: Full=4-aminobutyrate aminotransferase, PLP-dependent {ECO:0000313|EMBL:CAG70098.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:CAG70098.1};
GN Name=gabT {ECO:0000313|EMBL:CAG70098.1};
GN OrderedLocusNames=ACIAD3446 {ECO:0000313|EMBL:CAG70098.1};
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977 {ECO:0000313|EMBL:CAG70098.1, ECO:0000313|Proteomes:UP000000430};
RN [1] {ECO:0000313|EMBL:CAG70098.1, ECO:0000313|Proteomes:UP000000430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1 {ECO:0000313|Proteomes:UP000000430};
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG70098.1; -; Genomic_DNA.
DR RefSeq; WP_004923505.1; NC_005966.1.
DR AlphaFoldDB; Q6F767; -.
DR STRING; 202950.GCA_001485005_01757; -.
DR GeneID; 45235632; -.
DR KEGG; aci:ACIAD3446; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_6; -.
DR OrthoDB; 9801052at2; -.
DR BioCyc; ASP62977:ACIAD_RS15590-MONOMER; -.
DR Proteomes; UP000000430; 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; 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:CAG70098.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000000430};
KW Transferase {ECO:0000313|EMBL:CAG70098.1}.
SQ SEQUENCE 428 AA; 45946 MW; 148723FA290DE3DA CRC64;
MDTKHSALNQ RKQQATPRGV GVMCQWYADK AENATIWDAE GNTYIDFAGG IAVLNTGHRH
PKVLAAVKAQ LERFTHTAYQ VTPYESYVAL AERINELAPI AGPAKTTFFT TGAEAVENAV
KIARCYTGRQ GIITFGNGFH GRSFMTMAMT GKTAPYKRDF GLMPGGVFHA RYPVESRGIS
VDDALESIEN IFSEDVAPHD VAAIVLEPVQ GEGGFNVVPA DFLKRLRALC DKHGILLVAD
EVQTGFARTG KLYAMDHYET KADLITMAKS LGGGFPISGV VGRAEVMDAP NPGGLGGTYA
GNPVAVAAAH AVIDAIQEEK LCERANELGA ELVHVLKGLQ QSTDQVITDI RALGSMVAAE
FETAEQAKAV QNYAMQNGLL LLTCGKYGNV IRFLYPLTIP VEQFRSGLDI LKQGVASLAT
DHTTQAIG
//
