ID A0A109MVZ6_9BACI Unreviewed; 386 AA.
AC A0A109MVZ6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Pyridoxal phosphate-dependent aminotransferase {ECO:0000313|EMBL:KWW16561.1};
GN ORFNames=AS888_24345 {ECO:0000313|EMBL:KWW16561.1};
OS Peribacillus simplex.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX NCBI_TaxID=1478 {ECO:0000313|EMBL:KWW16561.1, ECO:0000313|Proteomes:UP000064189};
RN [1] {ECO:0000313|EMBL:KWW16561.1, ECO:0000313|Proteomes:UP000064189}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VanAntwerpen02 {ECO:0000313|EMBL:KWW16561.1,
RC ECO:0000313|Proteomes:UP000064189};
RA Couger M.B.;
RT "Genome Sequence of Bacillus simplex strain VanAntwerpen2.";
RL Submitted (NOV-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 DegT/DnrJ/EryC1 family.
CC {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
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:KWW16561.1}.
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DR EMBL; LNNH01000032; KWW16561.1; -; Genomic_DNA.
DR RefSeq; WP_061143295.1; NZ_LNNH01000032.1.
DR AlphaFoldDB; A0A109MVZ6; -.
DR Proteomes; UP000064189; Unassembled WGS sequence.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KWW16561.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Transferase {ECO:0000313|EMBL:KWW16561.1}.
FT ACT_SITE 191
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 191
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 386 AA; 42113 MW; 7BC6990A5F500BA7 CRC64;
MVQKRVFLSP PHMSGNEQYY VEQAFETNWI APLGPNVKAL EEGFAQYAGT NGALAVSSGT
SAIHLALKVL GVSRGDTVFC SSFTFIASAN PIVYQGAEPV FIDSEFDTWN MSPQALEIAL
DTAKKKRRIP KAVILVHLFG QSAKVEEIQS ICRKYKVALI EDAAESLGST FKGKQTGSFG
DMGIYSLNGN KIITASGGGM LVSDNEDYLD KALFLSTQAR DPAIHYEHSS VGYNYRLSNI
LAGVGRAQLE VLDDRVSARR GVFDRYQKSL GAIPGIAFMP ELKDTRGNRW LTAVIIDEKV
TGTRPIDIIH ALEAENIESR PLWKPLHLQP IFKGSAFFTA ADDIGVSSRL FEQGLCLPSG
SAMTKEDQDR IAAIVKEIAA PSKMTQ
//
