ID K2P4T0_9BACI Unreviewed; 438 AA.
AC K2P4T0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:EKF36122.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:EKF36122.1};
GN ORFNames=BA1_06882 {ECO:0000313|EMBL:EKF36122.1};
OS Bacillus xiamenensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1178537 {ECO:0000313|EMBL:EKF36122.1, ECO:0000313|Proteomes:UP000010122};
RN [1] {ECO:0000313|EMBL:EKF36122.1, ECO:0000313|Proteomes:UP000010122}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HYC-10 {ECO:0000313|EMBL:EKF36122.1,
RC ECO:0000313|Proteomes:UP000010122};
RX PubMed=23209239; DOI=10.1128/JB.01920-12;
RA Lai Q., Liu Y., Shao Z.;
RT "Genome Sequence of Bacillus sp. Strain HYC-10, Isolated from Intestinal
RT Tract Contents from a Marine Fish (Mugil cephalus).";
RL J. Bacteriol. 194:6991-6991(2012).
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:EKF36122.1}.
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DR EMBL; AMSH01000013; EKF36122.1; -; Genomic_DNA.
DR RefSeq; WP_008357047.1; NZ_LDHZ01000048.1.
DR AlphaFoldDB; K2P4T0; -.
DR KEGG; bxi:BK049_06040; -.
DR PATRIC; fig|1178537.3.peg.1408; -.
DR eggNOG; COG0160; Bacteria.
DR OrthoDB; 9807885at2; -.
DR Proteomes; UP000010122; 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 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:EKF36122.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:EKF36122.1}.
SQ SEQUENCE 438 AA; 47993 MW; 55131E527474BF9F CRC64;
MSQTTTNRFS TEEWQGKRDQ YVARGVSNGN RHLAAKGKGA ELFDIDGNRF IDFAGAIGTL
NVGHSHPKVV EAVKAQADSL IHPGFNVMMY ESYIELAEKL CHLTPGDHDK KAIFLNSGAE
AVENAVKIAR KYTKRQAVVS FTRGFHGRTN MTMSMTSKVK PYKFGFGPFA SEVYQAPYPY
YYQKPEGLSD AAYDDFIIDQ FNQFFIATVA PETVACVVME PVQGEGGFIV PSKRFVQHVA
SFCQQHGIVF VADEIQTGFA RTGKYFAIEH FDVVPDLITV SKSLAAGLPL SGVVGRKELL
DAADPGELGG TYAGSPLGCV AALAVLDIIE TEQLNQRSEH IGQVIEDKAN EWRTKYSFIG
EVRRLGAMAA IEMVEDQTTR TPDKKRAAAI AAYANKHGLL LLTAGINGNI IRFLTPLVIT
DELLHEGLGI IEDAFNAR
//
