ID C3GDI0_BACTU Unreviewed; 478 AA.
AC C3GDI0;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:EEM79594.1};
GN ORFNames=bthur0010_2950 {ECO:0000313|EMBL:EEM79594.1};
OS Bacillus thuringiensis serovar pondicheriensis BGSC 4BA1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=527029 {ECO:0000313|EMBL:EEM79594.1};
RN [1] {ECO:0000313|EMBL:EEM79594.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGSC 4BA1 {ECO:0000313|EMBL:EEM79594.1};
RX PubMed=22645259; DOI=10.1101/gr.134437.111;
RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT "Genomic characterization of the Bacillus cereus sensu lato species:
RT Backdrop to the evolution of Bacillus anthracis.";
RL Genome Res. 22:1512-1524(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:EEM79594.1}.
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DR EMBL; ACNH01000011; EEM79594.1; -; Genomic_DNA.
DR AlphaFoldDB; C3GDI0; -.
DR HOGENOM; CLU_016922_10_0_9; -.
DR Proteomes; UP000006660; Chromosome.
DR GO; GO:0003867; F:4-aminobutyrate transaminase activity; IEA:InterPro.
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:EEM79594.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:EEM79594.1}.
SQ SEQUENCE 478 AA; 52633 MW; 2B5100867B12C40A CRC64;
MEKNVGIHFA IKRENNVKKR MGYVMNTKKF AKVNEQIPGP KAASLLERRQ NIVPKGVSNG
IPTFVQSANG ALVTDVDGNQ YIDFAGAIGT INVGHCHPAV KEALHKQVDQ YIHTGFNVMM
YEPYIELAEK LAALAPGSFD KQVLFLNSGA EAVENAVKIA RKYTKRPGII AFSKGFHGRT
LMTMTMTSKV KPYKFGFGPF APEVYKAPFP YEYRRPEGLT EEQYDDFMIE EFKNFFISEV
APETIAAVVM EPVQGEGGFI VPSKKFVQEV RNICSEHGIL FVADEIQTGF SRTGKYFAID
HYDVVPDLIT VSKSLGAGVP ISGVIGRKEI MNESAPGELG GTYAGSPLGC AAALAVLDVI
EKENLNDRAI ELGKVVMNRF EEMKNKYNCI GDVRGLGAMC AFELVQDRKT KTPDKTLTAN
LCTEANKRGL LLLSAGTYGN VIRVLMPLVI TDEQLEEGLT IIEESLQICY EKANTARV
//
