ID   E4LDE9_9FIRM            Unreviewed;       399 AA.
AC   E4LDE9;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Aminotransferase, class I/II {ECO:0000313|EMBL:EFR60310.1};
DE            EC=2.6.1.- {ECO:0000313|EMBL:EFR60310.1};
GN   ORFNames=HMPREF9199_1119 {ECO:0000313|EMBL:EFR60310.1};
OS   Veillonella sp. oral taxon 158 str. F0412.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Veillonella.
OX   NCBI_TaxID=879309 {ECO:0000313|EMBL:EFR60310.1, ECO:0000313|Proteomes:UP000003565};
RN   [1] {ECO:0000313|EMBL:EFR60310.1, ECO:0000313|Proteomes:UP000003565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0412 {ECO:0000313|EMBL:EFR60310.1,
RC   ECO:0000313|Proteomes:UP000003565};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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:EFR60310.1}.
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DR   EMBL; AENU01000015; EFR60310.1; -; Genomic_DNA.
DR   AlphaFoldDB; E4LDE9; -.
DR   STRING; 879309.HMPREF9199_1119; -.
DR   eggNOG; COG1448; Bacteria.
DR   OrthoDB; 9766445at2; -.
DR   Proteomes; UP000003565; 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:0006520; P:amino acid metabolic process; IEA:InterPro.
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; IPR000796; Asp_trans.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11879; ASPARTATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11879:SF22; ASPARTATE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:EFR60310.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Transferase {ECO:0000313|EMBL:EFR60310.1}.
FT   DOMAIN          28..389
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   399 AA;  44307 MW;  67D54C049BD0CF07 CRC64;
     MIFVTAGQAL ADAKENGREN VINGTLGAIH DEDGKLVFLK TVKEEYLGLS DTEHIGYAPI
     AGVPEFLAAA EKECFGNSRP EGHIRSIATA GGTGGIHHLI HNYTEPGDEV LTADWYWGAY
     KVICSDIGRT LVTYSLFDEQ NNFNHEAFKN RVNELAARQT NVVILFNTPG NNPTGYSIED
     KDWDSILNFL KELVAIGRNN VIIGIDVAYL DFSGDREEVR GFFSKFGHLP KAILTCVCYS
     LSKGFTMYGQ RVGAMIGISD DEEIADEFLE INKNTSRATW SNICRPAMRT MANIVADPVK
     FKAYEEERNS YYQLIRDRAD IFKQEAAQVG LPMLPYRGGF FITIPTDSAN AICEELKKEH
     VYVIALAKGI RVAACGIPKF QMTGLATKIY NVMKRLGKL
//