(data stored in ACNUC7421 zone)

SWISSPROT: Q4WNL4_ASPFU

ID   Q4WNL4_ASPFU            Unreviewed;       411 AA.
AC   Q4WNL4;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 97.
DE   RecName: Full=Branched-chain-amino-acid aminotransferase {ECO:0000256|RuleBase:RU004517};
DE            EC=2.6.1.42 {ECO:0000256|RuleBase:RU004517};
GN   ORFNames=AFUA_4G06160 {ECO:0000313|EMBL:EAL90170.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL90170.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL90170.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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|RuleBase:RU004516};
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {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:EAL90170.1}.
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DR   EMBL; AAHF01000005; EAL90170.1; -; Genomic_DNA.
DR   RefSeq; XP_752208.1; XM_747115.1.
DR   STRING; 746128.CADAFUBP00006153; -.
DR   EnsemblFungi; EAL90170; EAL90170; AFUA_4G06160.
DR   GeneID; 3508922; -.
DR   KEGG; afm:AFUA_4G06160; -.
DR   EuPathDB; FungiDB:Afu4g06160; -.
DR   HOGENOM; HOG000276704; -.
DR   InParanoid; Q4WNL4; -.
DR   KO; K00826; -.
DR   OMA; LTEVFAC; -.
DR   OrthoDB; 853728at2759; -.
DR   Proteomes; UP000002530; Chromosome 4.
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:0052655; F:L-valine transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd01557; BCAT_beta_family; 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; IPR033939; BCAT_family.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   PIRSF; PIRSF006468; BCAT1; 1.
DR   SUPFAM; SSF56752; SSF56752; 1.
DR   TIGRFAMs; TIGR01123; ilvE_II; 1.
DR   PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4WNL4.
DR   SWISS-2DPAGE; Q4WNL4.
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004517};
KW   Aminotransferase {ECO:0000256|RuleBase:RU004517,
KW   ECO:0000313|EMBL:EAL90170.1};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|RuleBase:RU004517};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU004516};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Transferase {ECO:0000256|RuleBase:RU004517, ECO:0000313|EMBL:EAL90170.1}.
FT   MOD_RES         245
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006468-1"
SQ   SEQUENCE   411 AA;  45667 MW;  1B6424555299CE2B CRC64;
     MSSLRQLTRH RTLHSFASTR VRVQNPETRQ SWQRYFSATS AFASQQAGLD PSKLTVTKTT
     TPKELVAPKD LVFGKTFTDH MLSIEWSAAN GWNAPRIVPY QNLSLDPSAC VFHYAFECFE
     GMKAYKDKKG QIRLFRPDKN MARLNKSSER IALPTFDGDA LIKLIGEFVR LDSRFIPDAR
     GYSLYLRPTM IGTQNTLGVG PPGSALLFVI ASPVGPYYPT GFKAISLEAT DYAVRAWPGG
     VGDKKLGANY APCIVPQLKA ASRGFQQNLW LFGDEEYVTE VGTMNLFIAL KNKETGQKEL
     VTAPLDGTIL EGVTRDSVLA LARERLVPKG WTVSERKIRM SEVAEASEEG RLIEVFGAGT
     AAIVSPVRTI SYRGKMVDCG LKKNEEAGEV ALQMKNWIEG IQYGDEEHPW R
//

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