ID A0A0L0BJR7_9MICC Unreviewed; 464 AA.
AC A0A0L0BJR7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:KNC20326.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:KNC20326.1};
GN ORFNames=AC792_01260 {ECO:0000313|EMBL:KNC20326.1};
OS Arthrobacter sp. RIT-PI-e.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1681197 {ECO:0000313|EMBL:KNC20326.1, ECO:0000313|Proteomes:UP000053253};
RN [1] {ECO:0000313|Proteomes:UP000053253}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIT-PI-e {ECO:0000313|Proteomes:UP000053253};
RA Tan N.E.H., Lee Y.P., Gan H.M., Savka M.A.;
RT "Whole genome sequencing of endophytes isolated from poison ivy
RT (Toxicodendron radicans).";
RL Submitted (JUL-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNC20326.1}.
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DR EMBL; LGIU01000026; KNC20326.1; -; Genomic_DNA.
DR RefSeq; WP_049828782.1; NZ_LGIU01000026.1.
DR AlphaFoldDB; A0A0L0BJR7; -.
DR STRING; 1681197.AC792_01260; -.
DR PATRIC; fig|1681197.3.peg.2473; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000053253; Unassembled WGS sequence.
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:0000313|EMBL:KNC20326.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000053253};
KW Transferase {ECO:0000313|EMBL:KNC20326.1}.
SQ SEQUENCE 464 AA; 48423 MW; 80F664D25B5DFEDB CRC64;
MTTFATTAKI AAPTFRLEQR RHITGDFPGP RSAALAARRA AVVAKGVASG VPVYVADADG
GVVLDVDGNS FIDLGAGIAV TSVGASAPAV VDAVKDQVEH FTHTCFMVTP YEGYIAVAEQ
LADLTPGDFE KRTVLFNSGA EAVENAVKVA RLATGRNAVV AFDHAYHGRT NLTMALTAKS
MPYKSNFGPF APEIYRMPMS YPFREENPGI TGPEAAQRAI TMIEKQIGAD SVAAIIIEPV
QGEGGFIVPA EGFLPALADW AKANDVVFIA DEVQSGFCRT GAWFAVDHEG VVPDIITMAK
GIAGGMPLSA ITGRAELLDA VHVGGLGGTY GGNPVACAAA LGAIDTMKEQ DLAGRARHIE
AQVTERLGAL QADLGEDGII GEVRGRGAML ALEFVEQGGG RTPDAEVTKA IAARCLREGV
IVLTCGTYGN VVRLLPPLVI TDELLADALD VLEAAIRDAN EGRP
//
