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Database: UniProt/TrEMBL
Entry: Q4WHC3_ASPFU
LinkDB: Q4WHC3_ASPFU
Original site: Q4WHC3_ASPFU 
ID   Q4WHC3_ASPFU            Unreviewed;       490 AA.
AC   Q4WHC3;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   05-JUL-2017, entry version 79.
DE   RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE            EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN   ORFNames=AFUA_2G05910 {ECO:0000313|EMBL:EAL87682.1};
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:EAL87682.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL87682.1, 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.,
RA   Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.,
RA   Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S.,
RA   Farman M., Fedorova N., Fedorova N., Feldblyum T.V., Fischer R.,
RA   Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A.,
RA   Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.,
RA   Haas H., Harris D., Horiuchi H., Huang J., Humphray S., Jimenez J.,
RA   Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S.,
RA   Kulkarni R., Kumagai T., Lafon A., Latge J.P., Li W., Lord A., Lu C.,
RA   Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M.,
RA   Mouyna I., Mulligan S., Murphy L., O'Neil S., Paulsen I.,
RA   Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M.,
RA   Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S.,
RA   Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J.,
RA   White O., Woodward J., Yu J.H., Fraser C., Galagan J.E., Asai K.,
RA   Machida M., Hall N., Barrell B., 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 hexokinase family.
CC       {ECO:0000256|RuleBase:RU362007, ECO:0000256|SAAS:SAAS00672880}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EAL87682.1}.
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DR   EMBL; AAHF01000008; EAL87682.1; -; Genomic_DNA.
DR   RefSeq; XP_749720.1; XM_744627.1.
DR   ProteinModelPortal; Q4WHC3; -.
DR   STRING; 5085.CADAFUBP00002241; -.
DR   PRIDE; Q4WHC3; -.
DR   EnsemblFungi; CADAFUAT00003481; CADAFUAP00003481; CADAFUAG00003481.
DR   GeneID; 3506901; -.
DR   KEGG; afm:AFUA_2G05910; -.
DR   EuPathDB; FungiDB:Afu2g05910; -.
DR   HOGENOM; HOG000162670; -.
DR   InParanoid; Q4WHC3; -.
DR   KO; K00844; -.
DR   OMA; ERQFFRA; -.
DR   OrthoDB; EOG092C2JW4; -.
DR   Proteomes; UP000002530; Chromosome 2.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008865; F:fructokinase activity; IMP:AspGD.
DR   GO; GO:0004340; F:glucokinase activity; IDA:AspGD.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0046835; P:carbohydrate phosphorylation; IDA:AspGD.
DR   GO; GO:0001678; P:cellular glucose homeostasis; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001312; Hexokinase.
DR   InterPro; IPR019807; Hexokinase_BS.
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; PS00378; HEXOKINASE_1; 1.
DR   PROSITE; PS51748; HEXOKINASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362007,
KW   ECO:0000256|SAAS:SAAS00672869};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002530};
KW   Glycolysis {ECO:0000256|RuleBase:RU362007,
KW   ECO:0000256|SAAS:SAAS00672870};
KW   Kinase {ECO:0000256|RuleBase:RU362007, ECO:0000256|SAAS:SAAS00672871,
KW   ECO:0000313|EMBL:EAL87682.1};
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,
KW   ECO:0000256|SAAS:SAAS00672884, ECO:0000313|EMBL:EAL87682.1}.
FT   DOMAIN       27    221       Hexokinase_1. {ECO:0000259|Pfam:PF00349}.
FT   DOMAIN      227    466       Hexokinase_2. {ECO:0000259|Pfam:PF03727}.
SQ   SEQUENCE   490 AA;  54209 MW;  3FE75D900092404B CRC64;
     MVGIGPKRPP SRKGSMADVP QNLLQQIKDF EEMFTVDKAK LKQVVDHFVK ELDKGLSVEG
     GNIPMNVTWV MGFPDGDEQG TFLALDMGGT NLRVCEITLT EEKGGFDICQ SKYRMPEELK
     TGTAEELWEY IADCIQQFIE FHHGEEGLTS LPLGFTFSYP ATQEYIDHGI LQRWTKGFDI
     DGVEGQDVVP PLEETLKRKG LPIKVAALIN DTTGTLIASA YTDPEMKIGC IFGTGVNAAY
     MENVGSVPKL AHMNLPPDMP VAINCEYGAF DNEHVVLPLT KYDHIIDRDS PRPGQQAFEK
     MTAGLYLGEI FRLALIDLLD SRPGLIFQNQ DTSKLRKPYL LDASFLAAIE EDPYENLQET
     QELFERELNI KPTLAELEMI RRLAELIGTR AARLSACGVA AICKKKNIES CHVGADGSVF
     TKYPHFKARG AQALREILDW APNEKDKVTI MAAEDGSGVG AALIAALTLK RVKAGNLAGI
     RNKDEMQKLL
//
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