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Database: UniProt/TrEMBL
Entry: E3L723_PUCGT
LinkDB: E3L723_PUCGT
Original site: E3L723_PUCGT 
ID   E3L723_PUCGT            Unreviewed;       485 AA.
AC   E3L723;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 2.
DT   05-JUL-2017, entry version 41.
DE   RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE            EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN   ORFNames=PGTG_18333 {ECO:0000313|EMBL:EFP92346.2};
OS   Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
OS   (Black stem rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=418459 {ECO:0000313|EMBL:EFP92346.2, ECO:0000313|Proteomes:UP000008783};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CRL 75-36-700-3;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Cuomo C.,
RA   Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Mauceli E.,
RA   Brockman W., Young S., LaButti K., Sykes S., DeCaprio D., Crawford M.,
RA   Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C.,
RA   Larson L., White J., Zeng Q., Kodira C., Yandava C., Alvarado L.,
RA   O'Leary S., Szabo L., Dean R., Schein J.;
RT   "The Genome Sequence of Puccinia graminis f. sp. tritici Strain CRL
RT   75-36-700-3.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000008783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRL 75-36-700-3 / race SCCL
RC   {ECO:0000313|Proteomes:UP000008783};
RX   PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA   Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA   Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J.,
RA   Cantarel B.L., Chiu R., Coutinho P.M., Feau N., Field M., Frey P.,
RA   Gelhaye E., Goldberg J., Grabherr M.G., Kodira C.D., Kohler A.,
RA   Kuees U., Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E.,
RA   Murat C., Pangilinan J.L., Park R., Pearson M., Quesneville H.,
RA   Rouhier N., Sakthikumar S., Salamov A.A., Schmutz J., Selles B.,
RA   Shapiro H., Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y.,
RA   Rouze P., Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA   Grigoriev I.V., Szabo L.J., Martin F.;
RT   "Obligate biotrophy features unraveled by the genomic analysis of rust
RT   fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
CC   -!- SIMILARITY: Belongs to the hexokinase family.
CC       {ECO:0000256|RuleBase:RU362007, ECO:0000256|SAAS:SAAS00672880}.
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DR   EMBL; DS178363; EFP92346.2; -; Genomic_DNA.
DR   RefSeq; XP_003336765.2; XM_003336717.2.
DR   STRING; 5297.EFP92346; -.
DR   EnsemblFungi; EFP92346; EFP92346; PGTG_18333.
DR   GeneID; 10538010; -.
DR   KEGG; pgr:PGTG_18333; -.
DR   EuPathDB; FungiDB:PGTG_18333; -.
DR   InParanoid; E3L723; -.
DR   KO; K00844; -.
DR   OrthoDB; EOG092C2JW4; -.
DR   Proteomes; UP000008783; Unassembled WGS sequence.
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; 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:UP000008783};
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:EFP92346.2};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362007,
KW   ECO:0000256|SAAS:SAAS00672883};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008783};
KW   Transferase {ECO:0000256|RuleBase:RU362007,
KW   ECO:0000256|SAAS:SAAS00672884}.
FT   DOMAIN       30    228       Hexokinase_1. {ECO:0000259|Pfam:PF00349}.
FT   DOMAIN      234    472       Hexokinase_2. {ECO:0000259|Pfam:PF03727}.
SQ   SEQUENCE   485 AA;  53809 MW;  2ACB4AF7224CA3DB CRC64;
     MVVVLSLFIT RTHDNAQLPH ATKMQMADYL RKFEHLFMVT PQRMRMIVEA FIDTLEAGLK
     EDGQCVPMIP TFVFGWPTGK EVGPYLAVDL GGTNLRVCHV ELQGDGRFEI TQAKYKLTDE
     QKQQEGEKLF DFCAECLSKF VNDQYVDDDG NLLLDADIPL GFTFSYPCTQ KKIDHGELIR
     WTKGFGNPNV EGHDVGEIFS KSLKKFKVPV KLTAVINDTT GTLIASSYVD PATRIGVIFG
     TGCNAAYMEK VANIPKIASL GLPPDAEMAI NCEWGAFDSG THEHLPRTKY DLVIDETSNK
     PGEQAFEKMI AGLYLGEVFR LIVVEMIEEG ILFLGQNTYK MEKSYCFDTA FLSLIESDPT
     EELLTVTGLF THFFGLDTTI SERQFFRRLA ELIGTRSARL SACGIAAIVS KMGMVETGCG
     VATDGSLYNK YPQFPQRLHE ALVDIFGEKG RLIKTYHAED GSGVGSAIIA AMTKARLAEG
     KFTHV
//
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