ID   A0A3R6VYQ8_9CLOT        Unreviewed;       395 AA.
AC   A0A3R6VYQ8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=DXC26_13845 {ECO:0000313|EMBL:RHU80880.1};
OS   Clostridiaceae bacterium OM08-6BH.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae.
OX   NCBI_TaxID=2292274 {ECO:0000313|EMBL:RHU80880.1, ECO:0000313|Proteomes:UP000284832};
RN   [1] {ECO:0000313|EMBL:RHU80880.1, ECO:0000313|Proteomes:UP000284832}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OM08-6BH {ECO:0000313|EMBL:RHU80880.1,
RC   ECO:0000313|Proteomes:UP000284832};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-2018) 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:RHU80880.1}.
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DR   EMBL; QUKV01000009; RHU80880.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3R6VYQ8; -.
DR   Proteomes; UP000284832; 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:RHU80880.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000284832};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:RHU80880.1}.
FT   DOMAIN          30..380
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   395 AA;  44884 MW;  25EDAF01D65D4EA4 CRC64;
     MRNPLSETIV NIKPSGIRKF FDLVSEMNDK DVISLGVGEP DFDTPWHVRD EGIYSLEKGR
     TFYTSNSGLK ELREEICNYL DRRYQVSYDW HHETIVTVGG SEGIDIAMRA MLDPGDEVLI
     PQPSYVSYEP CAILAGGKPV IIELKAENEF RLTPEELLEY ITDKTKILVL PYPNNPTGAI
     MERADLEKIA EIVMEKDIFV LSDEIYSELS YKGDHVTIAS IPGMKERTIL INGFSKAYAM
     TGWRLGYACG PREIIEQMTK IHQFAIMCAP TTSQYAAVEA MRNGDADVAT MREAYDQRRR
     YLVNAFKEMG LECFEPYGAF YIFPCIKEFG MTSEEFAERF LKEEKVAVVP GTAFGDSGEG
     FLRISYAYSL QNLKAALERL DRFVKKLRAE QKEQA
//