ID   A2E498_TRIV3            Unreviewed;       339 AA.
AC   A2E498;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=Branched-chain-amino-acid aminotransferase {ECO:0000256|RuleBase:RU004517};
DE            EC=2.6.1.42 {ECO:0000256|RuleBase:RU004517};
GN   ORFNames=TVAG_139240 {ECO:0000313|EMBL:EAY12544.1};
OS   Trichomonas vaginalis (strain ATCC PRA-98 / G3).
OC   Eukaryota; Metamonada; Parabasalia; Trichomonadida; Trichomonadidae;
OC   Trichomonas.
OX   NCBI_TaxID=412133 {ECO:0000313|EMBL:EAY12544.1, ECO:0000313|Proteomes:UP000001542};
RN   [1] {ECO:0000313|EMBL:EAY12544.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=G3 {ECO:0000313|EMBL:EAY12544.1};
RA   Amadeo P., Zhao Q., Wortman J., Fraser-Liggett C., Carlton J.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EAY12544.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G3 {ECO:0000313|EMBL:EAY12544.1};
RX   PubMed=17218520; DOI=10.1126/science.1132894;
RA   Carlton J.M., Hirt R.P., Silva J.C., Delcher A.L., Schatz M., Zhao Q.,
RA   Wortman J.R., Bidwell S.L., Alsmark U.C.M., Besteiro S.,
RA   Sicheritz-Ponten T., Noel C.J., Dacks J.B., Foster P.G., Simillion C.,
RA   Van de Peer Y., Miranda-Saavedra D., Barton G.J., Westrop G.D., Mueller S.,
RA   Dessi D., Fiori P.L., Ren Q., Paulsen I., Zhang H., Bastida-Corcuera F.D.,
RA   Simoes-Barbosa A., Brown M.T., Hayes R.D., Mukherjee M., Okumura C.Y.,
RA   Schneider R., Smith A.J., Vanacova S., Villalvazo M., Haas B.J., Pertea M.,
RA   Feldblyum T.V., Utterback T.R., Shu C.L., Osoegawa K., de Jong P.J.,
RA   Hrdy I., Horvathova L., Zubacova Z., Dolezal P., Malik S.B.,
RA   Logsdon J.M. Jr., Henze K., Gupta A., Wang C.C., Dunne R.L., Upcroft J.A.,
RA   Upcroft P., White O., Salzberg S.L., Tang P., Chiu C.-H., Lee Y.-S.,
RA   Embley T.M., Coombs G.H., Mottram J.C., Tachezy J., Fraser-Liggett C.M.,
RA   Johnson P.J.;
RT   "Draft genome sequence of the sexually transmitted pathogen Trichomonas
RT   vaginalis.";
RL   Science 315:207-212(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate +
CC         L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42;
CC         Evidence={ECO:0000256|RuleBase:RU004517};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-
CC         glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42;
CC         Evidence={ECO:0000256|RuleBase:RU004517};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-
CC         glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42;
CC         Evidence={ECO:0000256|RuleBase:RU004517};
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; DS113300; EAY12544.1; -; Genomic_DNA.
DR   RefSeq; XP_001324767.1; XM_001324732.1.
DR   AlphaFoldDB; A2E498; -.
DR   STRING; 5722.A2E498; -.
DR   GeneID; 4770510; -.
DR   KEGG; tva:TVAG_2v0252230; -.
DR   VEuPathDB; TrichDB:TVAG_139240; -.
DR   VEuPathDB; TrichDB:TVAGG3_0252230; -.
DR   eggNOG; KOG0975; Eukaryota.
DR   InParanoid; A2E498; -.
DR   OMA; VGMNAAY; -.
DR   Proteomes; UP000001542; Unassembled WGS sequence.
DR   GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IBA:GO_Central.
DR   GO; GO:0052656; F:L-isoleucine transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052654; F:L-leucine transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050048; F:L-leucine:2-oxoglutarate aminotransferase activity; IEA:RHEA.
DR   GO; GO:0052655; F:L-valine transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd01557; BCAT_beta_family; 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; IPR005786; B_amino_transII.
DR   InterPro; IPR043132; BCAT-like_C.
DR   InterPro; IPR043131; BCAT-like_N.
DR   InterPro; IPR033939; BCAT_family.
DR   NCBIfam; TIGR01123; ilvE_II; 1.
DR   PANTHER; PTHR42825; AMINO ACID AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42825:SF2; BRANCHED-CHAIN-AMINO-ACID AMINOTRANSFERASE 3, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   PIRSF; PIRSF006468; BCAT1; 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   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004517};
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000256|RuleBase:RU004517};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|RuleBase:RU004517};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU004516};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001542};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004517}.
FT   MOD_RES         184
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006468-1"
SQ   SEQUENCE   339 AA;  37438 MW;  BBE3CADDAF07186C CRC64;
     MQPENIDWKT LGFGYVQTEW RYIAHWKDGK WDEGKLVDTP MLTIHEGSTA LHYGQECFEG
     LKAYRCKDGS INLFRPDQNA LRMQKSCTRL MMPHVSVEMF IDACRKVVKA NEKWLAPYGT
     GASLYLRPFM IGVGANLGVK PAPEYIFSVF CSPVGAYFKG GLKPTNFIVT TYDRAAPQGT
     GAAKVGGNYA ASLLPGFDAH DKKYGDCIYL DPATHTYIEE VGSANFFGIT KDNKFITPLS
     PSILPSITKY SLLHLAKERL GMEAIEGSIR IDSLDQFKEA GACGTAAVIS PIGGIKYGDK
     FHVFFSETEV GPITQKLYNE LVGIQYGDIP APEGWIVKV
//