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Database: UniProt
Entry: A0A1H7KA98_9FIRM
LinkDB: A0A1H7KA98_9FIRM
Original site: A0A1H7KA98_9FIRM 
ID   A0A1H7KA98_9FIRM        Unreviewed;       426 AA.
AC   A0A1H7KA98;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=dTDP-4-amino-4,6-dideoxygalactose transaminase {ECO:0000313|EMBL:SEK83821.1};
GN   ORFNames=SAMN04487770_103127 {ECO:0000313|EMBL:SEK83821.1};
OS   Butyrivibrio sp. ob235.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Butyrivibrio.
OX   NCBI_TaxID=1761780 {ECO:0000313|EMBL:SEK83821.1, ECO:0000313|Proteomes:UP000199418};
RN   [1] {ECO:0000313|EMBL:SEK83821.1, ECO:0000313|Proteomes:UP000199418}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OB235 {ECO:0000313|EMBL:SEK83821.1,
RC   ECO:0000313|Proteomes:UP000199418};
RA   de Groot N.N.;
RL   Submitted (OCT-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 DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
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DR   EMBL; FOBE01000003; SEK83821.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7KA98; -.
DR   Proteomes; UP000199418; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000390-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199418}.
FT   ACT_SITE        207
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         207
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   426 AA;  47716 MW;  5AD245267AFADC12 CRC64;
     MDRFEGIKRF ENKVWLSSPT MHGDELKWIN AAIEANWVST IGENINESER MIQEKVGRKY
     AIGLSSGTAA LHLAMRLAGE KLYGPKPANV GTLAGHKVFC SDMTFDATVN PVAYEGGEAV
     FIDTEYDSWN MSPEALEKAF EIYPDVKLIV VAYLYGTPGK ISEIREIADR HGALIIEDAA
     ESLGATYEGE QTGKFGDYSV ISFNGNKIIT GSSGGMLLTD SEADCHKVRK LSTQAREDAP
     WYQHEELGYN YRMSNIVAGV VRGQIPYLDE HIALKKKVYD RYKEGLKDLP VSMNPVPDNC
     EPNYWLSCMI IDKDAMCPHV RSERKALYNH EAGKSCPTEI LDAIASFNAE GRPIWKPMHM
     QPIYRNNIFV TAEGILRGRS NAYIDEGTAA DISMDIFERG LCLPSDIKMT EEEQDIVIDI
     IHRCFK
//
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