(data stored in SCRATCH zone)

SWISSPROT: Q4WD97_ASPFU

ID   Q4WD97_ASPFU            Unreviewed;       476 AA.
AC   Q4WD97;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 86.
DE   RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE            EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN   ORFNames=AFUA_6G03980 {ECO:0000313|EMBL:EAL85641.1};
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:EAL85641.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL85641.1, 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   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 1/4.
CC       {ECO:0000256|SAAS:SAAS01216704}.
CC   -!- SIMILARITY: Belongs to the hexokinase family.
CC       {ECO:0000256|RuleBase:RU362007, ECO:0000256|SAAS:SAAS00672880}.
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:EAL85641.1}.
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DR   EMBL; AAHF01000012; EAL85641.1; -; Genomic_DNA.
DR   RefSeq; XP_747679.1; XM_742586.1.
DR   STRING; 746128.CADAFUBP00009167; -.
DR   EnsemblFungi; EAL85641; EAL85641; AFUA_6G03980.
DR   GeneID; 3505347; -.
DR   KEGG; afm:AFUA_6G03980; -.
DR   EuPathDB; FungiDB:Afu6g03980; -.
DR   HOGENOM; HOG000162670; -.
DR   InParanoid; Q4WD97; -.
DR   KO; K00844; -.
DR   OMA; LMSCAFY; -.
DR   OrthoDB; 1153545at2759; -.
DR   UniPathway; UPA00109; UER00180.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008865; F:fructokinase activity; IBA:GO_Central.
DR   GO; GO:0004340; F:glucokinase activity; IBA:GO_Central.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0019158; F:mannokinase activity; IBA:GO_Central.
DR   GO; GO:0001678; P:cellular glucose homeostasis; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR   InterPro; IPR001312; Hexokinase.
DR   InterPro; IPR022673; Hexokinase_C.
DR   InterPro; IPR022672; Hexokinase_N.
DR   PANTHER; PTHR19443; PTHR19443; 1.
DR   Pfam; PF00349; Hexokinase_1; 1.
DR   Pfam; PF03727; Hexokinase_2; 1.
DR   PROSITE; PS51748; HEXOKINASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4WD97.
DR   SWISS-2DPAGE; Q4WD97.
KW   ATP-binding {ECO:0000256|RuleBase:RU362007, ECO:0000256|SAAS:SAAS00216502};
KW   Glycolysis {ECO:0000256|RuleBase:RU362007, ECO:0000256|SAAS:SAAS00216492};
KW   Kinase {ECO:0000256|RuleBase:RU362007, ECO:0000256|SAAS:SAAS00216507,
KW   ECO:0000313|EMBL:EAL85641.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362007,
KW   ECO:0000256|SAAS:SAAS00672883};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Transferase {ECO:0000256|RuleBase:RU362007, ECO:0000256|SAAS:SAAS00672884,
KW   ECO:0000313|EMBL:EAL85641.1}.
FT   DOMAIN          24..217
FT                   /note="Hexokinase_1"
FT                   /evidence="ECO:0000259|Pfam:PF00349"
FT   DOMAIN          224..462
FT                   /note="Hexokinase_2"
FT                   /evidence="ECO:0000259|Pfam:PF03727"
SQ   SEQUENCE   476 AA;  52637 MW;  DE8B644C6F3C541C CRC64;
     MEKGLRTQPD LLSGAPEKLV IALQGLEELF AADRFLLRKI TDHFVKEMEK GLSAEGGDIP
     MNVTWIMGYP TGKEQGKFLI LDMGGTSLRV SQAQLLGSDR DMESIQEKYS IPQSIKQGTA
     DDLWDFVADC VQKFLQSRLS ESERSKVLPL AFTFSYPVIQ SSIKVGVLQC WTKDFCVSGV
     EGHDVVFQLE AAFERKKIPV QVVALVNDTV GTLFAAAHRD QEVKIGSIAS TGCNAAYMEE
     VAAIPKIQSC GLPSGALVAI NTEYGAFDKS RRILPRTRFD DEIDRTSAHP GQQLYEKMVS
     GPYLGELLRL VMLELHEAKL LFVGQDVSCL RQPNALEVSL FPTLEEDISE CMENARKCLW
     EKTGLDPAPH ELKACRYLAE LVGTRAARLY SCGIAAICKK RNIERCHIGV DGSIFGHYQN
     YRKRAAQALR DIFAWPDDLE DPIVFGFYKD GSGVGAALIA ALALERSDGT VLSRTE
//

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