ID   A0A150FQM2_CLOPD        Unreviewed;       398 AA.
AC   A0A150FQM2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=JWYL7_0941 {ECO:0000313|EMBL:KXZ39866.1};
OS   [Clostridium] paradoxum JW-YL-7 = DSM 7308.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae.
OX   NCBI_TaxID=1121328 {ECO:0000313|EMBL:KXZ39866.1, ECO:0000313|Proteomes:UP000092605};
RN   [1] {ECO:0000313|EMBL:KXZ39866.1, ECO:0000313|Proteomes:UP000092605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JW-YL-7 {ECO:0000313|EMBL:KXZ39866.1,
RC   ECO:0000313|Proteomes:UP000092605};
RA   Utturkar S.M., Lancaster A., Poole F.L., Adams M.W., Brown S.D.;
RT   "Draft genome sequence for Clostridium paradoxum JW-YL-7.";
RL   Submitted (FEB-2016) 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:KXZ39866.1}.
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DR   EMBL; LSFY01000001; KXZ39866.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150FQM2; -.
DR   STRING; 1121328.JWYL7_0941; -.
DR   PATRIC; fig|1121328.3.peg.947; -.
DR   OrthoDB; 9802328at2; -.
DR   Proteomes; UP000092605; 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; ASPARTATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00753; ACCSYNTHASE.
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:KXZ39866.1};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:KXZ39866.1}.
FT   DOMAIN          31..384
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   398 AA;  45106 MW;  BE1521E800F7A080 CRC64;
     MKFSNRIVNM QASPIRKLVP YATKAKADGK KVYHLNIGQP DIKTPQSFFD AVKNFNEEVL
     EYSFSQGMPE LIDAIREYYK NYDMDFDQDE ILITNGGSEA LMFAIIAIAD AGDEILSPEP
     FYTNYNGFAS AVDVNIIPIT TKAENGFHLP SRNEIESVIT NKTRGIVLSN PGNPTGVVYT
     REEIEMLASI AKQHDLFIIA DEVYREFVYD GLEYTSFGNI KEIQDRVIIV DSVSKRYSAC
     GARIGSIASK NKELMQQILK LCQGRLCVPT LEQIGSIELY KTPKSYFEEV NAEYKRRRDL
     VYKKLCEMEG VICKEPKGAF YVNVKLPVEN AEDFVIWMLK DFDVDGETVM MAPSEGFYST
     PGLGKDEVRI AYILNEDDLT KAMDILKKGL ETYRNLNK
//