(data stored in SCRATCH zone)

SWISSPROT: Q4WCU8_ASPFU

ID   Q4WCU8_ASPFU            Unreviewed;       412 AA.
AC   Q4WCU8;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 82.
DE   RecName: Full=Aspartate aminotransferase {ECO:0000256|RuleBase:RU000480};
DE            EC=2.6.1.1 {ECO:0000256|RuleBase:RU000480};
GN   ORFNames=AFUA_6G02490 {ECO:0000313|EMBL:EAL85790.1};
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:EAL85790.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL85790.1, 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-aspartate = L-glutamate + oxaloacetate;
CC         Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC         Evidence={ECO:0000256|RuleBase:RU000480};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU000480}.
CC   -!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial and
CC       chloroplastic isozymes. {ECO:0000256|RuleBase:RU000480}.
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:EAL85790.1}.
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; AAHF01000012; EAL85790.1; -; Genomic_DNA.
DR   RefSeq; XP_747828.1; XM_742735.1.
DR   STRING; 746128.CADAFUBP00009314; -.
DR   EnsemblFungi; EAL85790; EAL85790; AFUA_6G02490.
DR   GeneID; 3505079; -.
DR   KEGG; afm:AFUA_6G02490; -.
DR   EuPathDB; FungiDB:Afu6g02490; -.
DR   HOGENOM; HOG000185898; -.
DR   InParanoid; Q4WCU8; -.
DR   KO; K14454; -.
DR   OMA; IACANER; -.
DR   OrthoDB; 1104596at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006532; P:aspartate biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR000796; Asp_trans.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR11879; PTHR11879; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00799; TRANSAMINASE.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   4: Predicted;
DR   PRODOM; Q4WCU8.
DR   SWISS-2DPAGE; Q4WCU8.
KW   Aminotransferase {ECO:0000256|RuleBase:RU000480,
KW   ECO:0000313|EMBL:EAL85790.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Transferase {ECO:0000256|RuleBase:RU000480, ECO:0000313|EMBL:EAL85790.1}.
FT   DOMAIN          29..405
FT                   /note="Aminotran_1_2"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   412 AA;  46012 MW;  3C7524DBFB0F4F26 CRC64;
     MSVLSTLAPV PPDEIFALNR AYATDPFPQK VSLGVGVYRT DDGKPWPLPC VREAEKQLLA
     EDSLTRHEYT AIEGDIPFLE LARDIMFGFD GKNAAEKHKS RIGSVQTVAG TGANHLGALF
     LATHMKPGKV WLSNPSWANH MTIWELAGVP RKTYPYYNPT TRSFDFDGMM ATLEAEAQQG
     DVILLHACAH NPTGLDPNKE QWKAIADLCE RKKIFPFFDS AYQGFASGSL EEDAWAVRYF
     LNEKPGMEMC VAQSFSKNFG LYGQRVGAFH YVLPQGSESL RDTVVVNLCH LIRGEYSMGP
     TAGCNLVKKV LTNEELTAQW HKDLKVMSSR IRSMRKALYD ELLRLQTPGS WRHIVEQNGM
     FSYTGLTPAQ VHSLKDKYHI YLLKSGRASI SGLSEKNVAY VAQAIDDVVR NV
//

If you have problems or comments...

PBIL Back to PBIL home page