(data stored in ACNUC7421 zone)

SWISSPROT: Q4WDM0_ASPFU

ID   Q4WDM0_ASPFU            Unreviewed;       330 AA.
AC   Q4WDM0;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 103.
DE   SubName: Full=Malate dehydrogenase, NAD-dependent {ECO:0000313|EMBL:EAL85518.1};
DE            EC=1.1.1.37 {ECO:0000313|EMBL:EAL85518.1};
GN   ORFNames=AFUA_6G05210 {ECO:0000313|EMBL:EAL85518.1};
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:EAL85518.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL85518.1, 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   -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC       {ECO:0000256|RuleBase:RU003369}.
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:EAL85518.1}.
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DR   EMBL; AAHF01000012; EAL85518.1; -; Genomic_DNA.
DR   RefSeq; XP_747556.1; XM_742463.1.
DR   STRING; 746128.CADAFUBP00009043; -.
DR   SwissPalm; Q4WDM0; -.
DR   PRIDE; Q4WDM0; -.
DR   EnsemblFungi; EAL85518; EAL85518; AFUA_6G05210.
DR   GeneID; 3505026; -.
DR   KEGG; afm:AFUA_6G05210; -.
DR   EuPathDB; FungiDB:Afu6g05210; -.
DR   HOGENOM; HOG000213792; -.
DR   InParanoid; Q4WDM0; -.
DR   KO; K00026; -.
DR   OMA; PRNHGFT; -.
DR   OrthoDB; 1204514at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 3.90.110.10; -; 1.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR022383; Lactate/malate_DH_C.
DR   InterPro; IPR001236; Lactate/malate_DH_N.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR010097; Malate_DH_type1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01772; MDH_euk_gproteo; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4WDM0.
DR   SWISS-2DPAGE; Q4WDM0.
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003369,
KW   ECO:0000313|EMBL:EAL85518.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530}.
FT   DOMAIN          3..146
FT                   /note="Ldh_1_N"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          148..324
FT                   /note="Ldh_1_C"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        179
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         88
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         120
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         154
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ   SEQUENCE   330 AA;  34810 MW;  9164FA145DAFB42F CRC64;
     MVKAAVLGAS GGIGQPLSLL LKACPLVDEL ALYDVVNTPG VAADLSHISS VAKVSGYLPK
     DDGLKNALTG TDIVVIPAGI PRKPGMTRDD LFKVNAGIVR DLVTGIAQYC PKAFVLIISN
     PVNSTVPIAA EVLKKQGVFD PKRLFGVTTL DIVRAETFTQ EYSGQKDPSK VQIPVVGGHS
     GETIVPLFSK ASPALDIPAD KYDALVNRVQ FGGDEVVKAK DGAGSATLSM AYAGFRFAEK
     VIRASQGQSG IVEPTYIYLR GVTGGEEIAN ETGVEFFSTL VELGRNGAEK AINILQGVTE
     QEKKLLEACT KGLKGNIEKG IEFVKNTPPK
//

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