(data stored in SCRATCH zone)

SWISSPROT: Q4WD53_ASPFU

ID   Q4WD53_ASPFU            Unreviewed;       539 AA.
AC   Q4WD53;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 91.
DE   RecName: Full=Malate synthase {ECO:0000256|RuleBase:RU000555};
DE            EC=2.3.3.9 {ECO:0000256|RuleBase:RU000555};
GN   ORFNames=AFUA_6G03540 {ECO:0000313|EMBL:EAL85685.1};
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:EAL85685.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL85685.1, 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=acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+);
CC         Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288; EC=2.3.3.9;
CC         Evidence={ECO:0000256|RuleBase:RU000555};
CC   -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC       isocitrate: step 2/2. {ECO:0000256|RuleBase:RU000555}.
CC   -!- SIMILARITY: Belongs to the malate synthase family.
CC       {ECO:0000256|RuleBase:RU000555}.
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:EAL85685.1}.
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DR   EMBL; AAHF01000012; EAL85685.1; -; Genomic_DNA.
DR   RefSeq; XP_747723.1; XM_742630.1.
DR   STRING; 746128.CADAFUBP00009209; -.
DR   PRIDE; Q4WD53; -.
DR   EnsemblFungi; EAL85685; EAL85685; AFUA_6G03540.
DR   GeneID; 3505008; -.
DR   KEGG; afm:AFUA_6G03540; -.
DR   EuPathDB; FungiDB:Afu6g03540; -.
DR   HOGENOM; HOG000238464; -.
DR   InParanoid; Q4WD53; -.
DR   KO; K01638; -.
DR   OMA; MENVRAD; -.
DR   OrthoDB; 358540at2759; -.
DR   UniPathway; UPA00703; UER00720.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005782; C:peroxisomal matrix; IBA:GO_Central.
DR   GO; GO:0004474; F:malate synthase activity; IBA:GO_Central.
DR   GO; GO:0006097; P:glyoxylate cycle; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   CDD; cd00727; malate_synt_A; 1.
DR   InterPro; IPR011076; Malate_synth-like_sf.
DR   InterPro; IPR006252; Malate_synthA.
DR   InterPro; IPR001465; Malate_synthase.
DR   InterPro; IPR019830; Malate_synthase_CS.
DR   PANTHER; PTHR42902; PTHR42902; 1.
DR   Pfam; PF01274; Malate_synthase; 1.
DR   PIRSF; PIRSF001363; Malate_synth; 1.
DR   SUPFAM; SSF51645; SSF51645; 1.
DR   TIGRFAMs; TIGR01344; malate_syn_A; 1.
DR   PROSITE; PS00510; MALATE_SYNTHASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4WD53.
DR   SWISS-2DPAGE; Q4WD53.
KW   Acyltransferase {ECO:0000313|EMBL:EAL85685.1};
KW   Glyoxylate bypass {ECO:0000256|RuleBase:RU000555};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Transferase {ECO:0000256|RuleBase:RU000555, ECO:0000313|EMBL:EAL85685.1};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU000555}.
FT   ACT_SITE        168
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
FT   ACT_SITE        449
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
SQ   SEQUENCE   539 AA;  61060 MW;  42D4C0E1E36F1E9E CRC64;
     MSQIEVQLKD VAILGAVNNE HRKILTKEAC AFLAILHRTF NPTRKALLQR RIDRQAEIDK
     GHLPDFLPET KHIRENDAWK GAPPAPGLVD RRVEITGPTD RKMVVNALNA DVWTYMADFE
     DSSAPTWANM INGQVNLYDA IRRQIDFKQG NKEYKLRTDR ALPTLIARAR GWHLDEKHFT
     VDGEPISGSL FDFGLYFFHN AKELVARGHG PYFYLPKMES HLEARLWNDV FNLAQDYIGM
     PRGTIRATVL IETITAAFEM DEIIYELRDH SSGLNCGRWD YIFSFIKKFR KHPNFVLPDR
     SDVTMTVPFM DAYVKLLIKT CHRRGVHAMG GMAAQIPIKD DPVANDKAME SVRADKLREV
     RAGHDGTWVA HPALASIASE VFNKYMPTPN QLFVRRQDVN ITANDLLNTN VPGKITEEGI
     RKNLNIGLSY MEGWLRGVGC IPINYLMEDA ATAEVSRSQL WQWVHHQVTS SEGKKIDKAY
     ALRLLQEQAD SLAAKSPKGN KFQLAARYFA GQVTGEDYAD FLTSLLYNEI STPGTASKL
//

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