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Entry: A0A0C9N9I1_9FUNG
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ID   A0A0C9N9I1_9FUNG        Unreviewed;       384 AA.
AC   A0A0C9N9I1;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Branched-chain-amino-acid aminotransferase {ECO:0000256|RuleBase:RU004517};
DE            EC=2.6.1.42 {ECO:0000256|RuleBase:RU004517};
GN   ORFNames=MAM1_0575d10949 {ECO:0000313|EMBL:GAN11388.1};
OS   Mucor ambiguus.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN11388.1};
RN   [1] {ECO:0000313|EMBL:GAN11388.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN11388.1};
RA   Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT   "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT   ambiguus NBRC6742.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; DF836864; GAN11388.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9N9I1; -.
DR   STRING; 91626.A0A0C9N9I1; -.
DR   OrthoDB; 1304at2759; -.
DR   Proteomes; UP000053815; Unassembled WGS sequence.
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; PTHR11825:SF44; BRANCHED-CHAIN-AMINO-ACID AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11825; SUBGROUP IIII AMINOTRANSFERASE; 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|ARBA:ARBA00022605,
KW   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:UP000053815};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004517}.
FT   MOD_RES         215
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006468-1"
SQ   SEQUENCE   384 AA;  42943 MW;  68FEAF38816AB9F6 CRC64;
     MFSSRILPSF KRSAFLQAKR FTSELSASKL QIKKADTLKP LVANNELVFG NTFTDHMISV
     DWDEKNGWAA PQLHPYENLS LAPSAVVFHY ASEAYKDEHG KIRLFRPDMN MARMNRSTAR
     IALPQFDGDE LIKIIGEYLK TDERWIPEGK GYSLYLRPTM IGTQEVLGVN PPTKAKLFVI
     GCPVGPYYKT GFNAVRLLAT TEYVRAWPRG TGEAKIGGNY APGLLPQRLA AEKGYQQNLW
     LFGEQHQLTE VGTMNLFVLL KNDNGDLELV TPPLDGSILP GVTRDSIIGL AKEWNEFEVK
     ERTMTMPELR DLAKAGRVVE MFGAGTACVV SPIKEIGYMG EDIKIPLDPK DAQSQAGPYT
     RRFNDAINAI QYGEVEHPWS VVVN
//
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