ID   R6FQU0_9CLOT            Unreviewed;       533 AA.
AC   R6FQU0;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=BN542_00780 {ECO:0000313|EMBL:CDB15553.1};
OS   Clostridium sp. CAG:221.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262780 {ECO:0000313|EMBL:CDB15553.1, ECO:0000313|Proteomes:UP000018176};
RN   [1] {ECO:0000313|EMBL:CDB15553.1, ECO:0000313|Proteomes:UP000018176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:221 {ECO:0000313|Proteomes:UP000018176};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDB15553.1}.
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DR   EMBL; CBDC010000067; CDB15553.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6FQU0; -.
DR   Proteomes; UP000018176; 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:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 1.10.20.110; -; 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; IPR022518; Aspartate_4-decarboxylase.
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   NCBIfam; TIGR03801; asp_4_decarbox; 1.
DR   PANTHER; PTHR43795:SF10; AMINOTRAN_1_2 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43795; BIFUNCTIONAL ASPARTATE AMINOTRANSFERASE AND GLUTAMATE/ASPARTATE-PREPHENATE AMINOTRANSFERASE-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:CDB15553.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:CDB15553.1}.
FT   DOMAIN          190..511
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   533 AA;  61073 MW;  5F216D7004CB3CBF CRC64;
     MNLQKDELRK VYGQISPFEF KDKLIRLAKA NNDDILDAGR GNPNWTASTP REAFFTFGQF
     AIKETQRTWC KDDLAGMPEK KNISKRFKEF LENSPETSAI ELLANILKYG IEEMNFDADE
     YIYELTDGII GDNYPVPDRM LIHIEKIVHN YLMKELCQNK KFESNFEVFA VEGGTAAMCY
     IFDSLVVNNL LKSGDTIALM TPIFTPYLEI PHLPNYKFNV INIKANEVDE NGNPTWQYPK
     EELNKLKDKN IKVLFVVNPN NPASIALSRD CKDNLISVVK EHNPELMIVT DDVYCTFVDN
     FNSLVSELPY NTLGVYSYSK YFGVTGWRLG TIFLNEKNIF NDLIKKLSPA MKNELNERYK
     HLCQNPTELS FMDRLVADSR QVALNHTAGL STPQQVQMAF FSLFALIDKE NTYKQLTKDI
     CKSRKDLLFN GLELEYEKSR HDAAYYTELN ILDIASMKYG NTFAQHIKEN YSTFDVLYDL
     AKEHGVILLN GDGFASSKWS IRVSLANLKD GAYPQIGTAI KNLIDNIYNS YIS
//