ID   A0A0K0GC17_9FIRM        Unreviewed;       391 AA.
AC   A0A0K0GC17;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=WH51_03955 {ECO:0000313|EMBL:KKE80068.1};
OS   Bacilli bacterium VT-13-104.
OC   Bacteria; Bacillota; Bacilli.
OX   NCBI_TaxID=1637974 {ECO:0000313|EMBL:KKE80068.1, ECO:0000313|Proteomes:UP000034981};
RN   [1] {ECO:0000313|Proteomes:UP000034981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VT-13-104 {ECO:0000313|Proteomes:UP000034981};
RA   Tetz V., Tetz G.;
RT   "Bacilli bacterium VT-13-104.";
RL   Submitted (APR-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         ECO:0000256|RuleBase:RU000481};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU000481}.
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:KKE80068.1}.
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DR   EMBL; LAZH01000020; KKE80068.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K0GC17; -.
DR   PATRIC; fig|1637974.4.peg.821; -.
DR   OrthoDB; 9802328at2; -.
DR   Proteomes; UP000034981; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR46383:SF5; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW   ECO:0000313|EMBL:KKE80068.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034981};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:KKE80068.1}.
FT   DOMAIN          33..382
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   391 AA;  43440 MW;  57D27911EC715626 CRC64;
     MSMDYEQYLS KTAIDLKPSG IRRFFDLAAS MEGVISLGVG EPDFITPWNI RDEAINALQD
     GYTSYTANAG LIELRQEISN YVQRRFDVHY DPENQIIVTV GASQSLDLAF RAIVNPGDEV
     LIVEPAFVSY ASLVLLAGGV PVPISTYSDN GFKVTPEQIE AAITDKTKAV LICTPNNPTG
     TCLNKEELTQ IANVIQKHDL ICLTDEIYAE LTYDDDGFTS MASIPGMYER TILINGFSKG
     FAMTGWRLGF VAAPKEMVDL MVKIYQYTTM CAPHMLQRAA IEALQNSTDQ VEHMRESYWR
     RRNYIVQALN NIGLSCHIPG GAFYVFPSIK QTGLSSEEFA SELLQQEKVA VVPGNAFGES
     GEGYIRCSYA TSIEQLQEAM KRMGRFIDSL K
//