ID   W2BYI5_9FIRM            Unreviewed;       399 AA.
AC   W2BYI5;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=HMPREF0378_0571 {ECO:0000313|EMBL:ETJ99286.1};
OS   Eubacterium nodatum ATCC 33099.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Eubacteriales Family XIII. Incertae Sedis.
OX   NCBI_TaxID=1161902 {ECO:0000313|EMBL:ETJ99286.1, ECO:0000313|Proteomes:UP000018868};
RN   [1] {ECO:0000313|EMBL:ETJ99286.1, ECO:0000313|Proteomes:UP000018868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33099 {ECO:0000313|EMBL:ETJ99286.1,
RC   ECO:0000313|Proteomes:UP000018868};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (DEC-2013) 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:ETJ99286.1}.
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DR   EMBL; AZKM01000024; ETJ99286.1; -; Genomic_DNA.
DR   AlphaFoldDB; W2BYI5; -.
DR   STRING; 1161902.HMPREF0378_0571; -.
DR   PATRIC; fig|1161902.3.peg.1250; -.
DR   eggNOG; COG0436; Bacteria.
DR   OrthoDB; 9802328at2; -.
DR   Proteomes; UP000018868; 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:SF2; (5-FORMYLFURAN-3-YL)METHYL PHOSPHATE TRANSAMINASE; 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:ETJ99286.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018868};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:ETJ99286.1}.
FT   DOMAIN          31..384
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   399 AA;  44347 MW;  E11B85F83BEF092E CRC64;
     MDISNRVESM QFSPIRKFNP IAIKAEKAGK KIYHLNIGQP DVETPECFMD AIRNFDEKVI
     AYAESGGRPE LIEAVKDYYK TYDISLESSD IMVTNGGSEA LSMTFITLLN EGDEVLVPEP
     YYTNYSTFAL MAGGVVKPVT TSAEDGYFYA DAARIEACIT PKTKAICCLE PGNPTGNVLT
     LDEMRVICEV AEKHDLMIIA DEVYREFVYD GRTPASFGQL EEYADRVIII DSVSKRFSAC
     GARIGLCISK NKEFMSGIMK IAQGRLCVST VDQIGSAALF RLPQSYYDEV KAEYCGRRDV
     VVEELNKIPG FSATVPGGAF YMTCKLPVDD IEDFLIFLLE EFEDNGESVM FAPAEGFYAT
     PGLGKDEIRI AYVLNQDDMK RGVELIRLGL EAYNKKLGK
//