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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//