ID   A0A1H4BF12_9FIRM        Unreviewed;       396 AA.
AC   A0A1H4BF12;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=SAMN02910384_01555 {ECO:0000313|EMBL:SEA46730.1};
OS   Pseudobutyrivibrio sp. ACV-2.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Pseudobutyrivibrio.
OX   NCBI_TaxID=1520801 {ECO:0000313|EMBL:SEA46730.1, ECO:0000313|Proteomes:UP000199179};
RN   [1] {ECO:0000313|Proteomes:UP000199179}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACV-2 {ECO:0000313|Proteomes:UP000199179};
RA   Varghese N., Submissions S.;
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|RuleBase:RU000481};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU000481}.
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DR   EMBL; FNQZ01000006; SEA46730.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H4BF12; -.
DR   STRING; 1520801.SAMN02910384_01555; -.
DR   OrthoDB; 9802328at2; -.
DR   Proteomes; UP000199179; 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; 2.
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; PTHR42691; ASPARTATE AMINOTRANSFERASE YHDR-RELATED; 1.
DR   PANTHER; PTHR42691:SF1; ASPARTATE AMINOTRANSFERASE YHDR-RELATED; 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:SEA46730.1};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:SEA46730.1}.
FT   DOMAIN          61..385
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   396 AA;  44208 MW;  67384A8F32A5AE78 CRC64;
     MINATYKKML EGKSIIRELS EYATARGKEI GYENVFDYSL GNPSVPCPKG YTDTVINMYQ
     NNDPMSIHGY SPSLGIEDVR EAVADSLKSR FDVPYEAKHI FMAIGAAGAL AHAFRLVTEP
     GDEIIVFAPF FPEYTEYIGR TGAVMKVVPP STKDFQINFD AFVDIINEKT MAVLINTPNN
     PTGIVYSEET IKRLAEILYA KQEEYGHDIF LISDEPYREI VFDGKVCPYP AKYYDNTLTC
     YSFSKSLSLP GERIGYVAVN PKATDSDILA VIMGQISRGI GHNCPSSTSQ LAVAQVLGET
     SDLSVYETNM NILYDALTEM GFEVVRPGGT FYIFPKALEE DANAFCSKAK KYDLILVPAD
     NFGCPGYFRM AYCIDTEKVR RSIAAFKRFV SEEYHK
//