ID   R6GNM1_9CLOT            Unreviewed;       245 AA.
AC   R6GNM1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Branched-chain amino acid aminotransferase {ECO:0000313|EMBL:CDB15767.1};
GN   ORFNames=BN542_00971 {ECO:0000313|EMBL:CDB15767.1};
OS   Clostridium sp. CAG:221.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262780 {ECO:0000313|EMBL:CDB15767.1, ECO:0000313|Proteomes:UP000018176};
RN   [1] {ECO:0000313|EMBL:CDB15767.1, 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:RU004516};
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00009320,
CC       ECO:0000256|RuleBase:RU004106}.
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:CDB15767.1}.
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DR   EMBL; CBDC010000076; CDB15767.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6GNM1; -.
DR   Proteomes; UP000018176; Unassembled WGS sequence.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046394; P:carboxylic acid biosynthetic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd00449; PLPDE_IV; 1.
DR   Gene3D; 3.30.470.10; -; 1.
DR   Gene3D; 3.20.10.10; D-amino Acid Aminotransferase, subunit A, domain 2; 1.
DR   InterPro; IPR001544; Aminotrans_IV.
DR   InterPro; IPR018300; Aminotrans_IV_CS.
DR   InterPro; IPR036038; Aminotransferase-like.
DR   InterPro; IPR043132; BCAT-like_C.
DR   InterPro; IPR043131; BCAT-like_N.
DR   PANTHER; PTHR42743; AMINO-ACID AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42743:SF24; AMINODEOXYCHORISMATE LYASE; 1.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:CDB15767.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU004516}; Transferase {ECO:0000313|EMBL:CDB15767.1}.
SQ   SEQUENCE   245 AA;  28658 MW;  E4BD691223544055 CRC64;
     MREISYNKDY VKLDGGFYFA QGVFETILIK EEAVFLEEHI NRLNKSIDIM GLGEHIDIEF
     IKNFIKQEKL KNIVLKIVVT EKNIVFSTRK IKYSKKDYKN GFKLKLSSVL RNPTSMMTYL
     KALSYNENLY EYNKANKEGF NEVVFLNIYG NIAEGATSNI FIIKDKKIYT PKISDGILPG
     VVRNWVIKNF KVCEKHLDKK DLYSADEVFI TNSILGIMKI VQFEERSYST SMVERIRSEY
     EQFII
//