ID A0A160M8B1_9BACI Unreviewed; 439 AA.
AC A0A160M8B1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:AND38564.1};
GN ORFNames=A361_05320 {ECO:0000313|EMBL:AND38564.1};
OS Cytobacillus oceanisediminis 2691.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Cytobacillus.
OX NCBI_TaxID=1196031 {ECO:0000313|EMBL:AND38564.1, ECO:0000313|Proteomes:UP000077856};
RN [1] {ECO:0000313|EMBL:AND38564.1, ECO:0000313|Proteomes:UP000077856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2691 {ECO:0000313|EMBL:AND38564.1,
RC ECO:0000313|Proteomes:UP000077856};
RA Jeong H., Kim H.J., Lee D.-W.;
RT "Complete genome sequence of Bacillus oceanisediminis strain 2691.";
RL Submitted (APR-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; CP015506; AND38564.1; -; Genomic_DNA.
DR RefSeq; WP_019382574.1; NZ_CP015506.1.
DR AlphaFoldDB; A0A160M8B1; -.
DR STRING; 1196031.A361_05320; -.
DR KEGG; bon:A361_05320; -.
DR eggNOG; COG0160; Bacteria.
DR Proteomes; UP000077856; Chromosome.
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 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:AND38564.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:AND38564.1}.
SQ SEQUENCE 439 AA; 48063 MW; 3428D0B9751C5DA3 CRC64;
MNEENWGHLV GNISNLLAPS MAKDHPNLPV VKAEGCYYYG VDGKEYLDFT SGIAVENVGH
RHPKVVQAIK DSADHLVHGP SGVIIYESIL RLADELGKIT PGNLDCFFFA NSGTEAIEGA
IKLAKYVTRR PYVISFTGCF HGRSMGALSV STSKSKYRKF QQPSWLTYQL PYADERDCPF
GEDPEEYFPR KLEEDAETLF KHQVDPEEVA CMIIEPVLGE GGYIIPPKKW MLKIREICDR
HGILLIFDEV QTGFGRTGEW FAAQAFDVVP DIMAIAKGIA AGLPLSATAA SKELMEKWPL
GAHGTTFGGN PIACSAALAS LEILKTENLL ENAKQMGEYA LKKLQDLKAE HPAIGSVRGL
GLMIGIEIID PQTGKPDGKA VMDILNSSLD KGVLFYLCGN SGEVIRMIPP LIVTKEQIDQ
GLKVLEEALT EHEAVVSNS
//
