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Database: UniProt
Entry: F7V2R3_CLOSS
LinkDB: F7V2R3_CLOSS
Original site: F7V2R3_CLOSS 
ID   F7V2R3_CLOSS            Unreviewed;       251 AA.
AC   F7V2R3;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Branched-chain amino acid aminotransferase {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=CXIVA_10750 {ECO:0000313|EMBL:BAK47042.1};
OS   Clostridium sp. (strain SY8519).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1042156 {ECO:0000313|EMBL:BAK47042.1, ECO:0000313|Proteomes:UP000008937};
RN   [1] {ECO:0000313|Proteomes:UP000008937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SY8519 {ECO:0000313|Proteomes:UP000008937};
RX   PubMed=21914882; DOI=10.1128/JB.05637-11;
RA   Yokoyama S., Oshima K., Nomura I., Hattori M., Suzuki T.;
RT   "Complete genomic sequence of the O-desmethylangolensin-producing bacterium
RT   Clostridium rRNA cluster XIVa strain SY8519, isolated from adult human
RT   intestine.";
RL   J. Bacteriol. 193:5568-5569(2011).
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}.
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DR   EMBL; AP012212; BAK47042.1; -; Genomic_DNA.
DR   RefSeq; WP_013977008.1; NC_015737.1.
DR   AlphaFoldDB; F7V2R3; -.
DR   STRING; 1042156.CXIVA_10750; -.
DR   KEGG; cls:CXIVA_10750; -.
DR   eggNOG; COG0115; Bacteria.
DR   HOGENOM; CLU_020844_2_0_9; -.
DR   OrthoDB; 9805628at2; -.
DR   Proteomes; UP000008937; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0046394; P:carboxylic acid biosynthetic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU004516};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008937}.
SQ   SEQUENCE   251 AA;  28948 MW;  D8C9CADFCC4A6878 CRC64;
     MNIQLDDGVQ FGLGAFETIA LQENTPLFLD WHLERLRRSL EFLHISQKVN AEEVIRWIDQ
     NAAKEPGSGQ EQRACKFMVS EKNKIFSLRK NPYTEAVKDR GFRLAYSPVL RNETSPLVYH
     KTMNYGDNIL EKRRTKNLPI DEVVFLNTRG ELCEGSTTNL FFVKQGQIFT PKQSCGLLPG
     ILRRYVLQTF FCRETVLYPR DAEQMEECFV TNSLMGIMPV LELGDVCYAR GPVTERCMER
     YRKDTEAAVT A
//
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