GenomeNet

Database: UniProt
Entry: Q887K3_PSESM
LinkDB: Q887K3_PSESM
Original site: Q887K3_PSESM 
ID   Q887K3_PSESM            Unreviewed;       321 AA.
AC   Q887K3;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Glucokinase {ECO:0000256|HAMAP-Rule:MF_00524};
DE            EC=2.7.1.2 {ECO:0000256|HAMAP-Rule:MF_00524};
DE   AltName: Full=Glucose kinase {ECO:0000256|HAMAP-Rule:MF_00524};
GN   Name=glk {ECO:0000256|HAMAP-Rule:MF_00524,
GN   ECO:0000313|EMBL:AAO54813.1};
GN   OrderedLocusNames=PSPTO_1289 {ECO:0000313|EMBL:AAO54813.1};
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283 {ECO:0000313|EMBL:AAO54813.1, ECO:0000313|Proteomes:UP000002515};
RN   [1] {ECO:0000313|EMBL:AAO54813.1, ECO:0000313|Proteomes:UP000002515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000 {ECO:0000313|Proteomes:UP000002515};
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., Deboy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Daugherty S., Brinkac L., Beanan M.J., Haft D.H., Nelson W.C., Davidsen T.,
RA   Zafar N., Zhou L., Liu J., Yuan Q., Khouri H., Fedorova N., Tran B.,
RA   Russell D., Berry K., Utterback T., Van Aken S.E., Feldblyum T.V.,
RA   D'Ascenzo M., Deng W.L., Ramos A.R., Alfano J.R., Cartinhour S.,
RA   Chatterjee A.K., Delaney T.P., Lazarowitz S.G., Martin G.B.,
RA   Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M., Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+);
CC         Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.2;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00524};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00524}.
CC   -!- SIMILARITY: Belongs to the bacterial glucokinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00524, ECO:0000256|RuleBase:RU004046}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016853; AAO54813.1; -; Genomic_DNA.
DR   RefSeq; NP_791118.1; NC_004578.1.
DR   RefSeq; WP_005764052.1; NC_004578.1.
DR   AlphaFoldDB; Q887K3; -.
DR   STRING; 223283.PSPTO_1289; -.
DR   GeneID; 1182925; -.
DR   KEGG; pst:PSPTO_1289; -.
DR   PATRIC; fig|223283.9.peg.1312; -.
DR   eggNOG; COG0837; Bacteria.
DR   HOGENOM; CLU_042582_1_0_6; -.
DR   OrthoDB; 9800595at2; -.
DR   PhylomeDB; Q887K3; -.
DR   Proteomes; UP000002515; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004340; F:glucokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.40.367.20; -; 1.
DR   HAMAP; MF_00524; Glucokinase; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR003836; Glucokinase.
DR   NCBIfam; TIGR00749; glk; 1.
DR   PANTHER; PTHR47690; GLUCOKINASE; 1.
DR   PANTHER; PTHR47690:SF1; GLUCOKINASE; 1.
DR   Pfam; PF02685; Glucokinase; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00524};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00524};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_00524};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00524};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00524};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002515};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00524}.
FT   BINDING         7..12
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00524"
SQ   SEQUENCE   321 AA;  34317 MW;  888083844CAF35F2 CRC64;
     MKLALVGDIG GTNARFAIWE DDTLHSVRVF PTIDYAGPEK AIEVYLQDLE LQRGDIGYVC
     LAVAGPVDGD LFQFTNSHWQ LSREAFCADL KVDHLLLIND FTAMALGMTR LKDDEYLTVC
     HGVGKPDRPR VVVGPGTGLG IGTLIKLEDS RWMALPGEGG HADLPIGTAR EALLWTRLMA
     EHEHVSAEVV LSGAGLLLLY QVSCALDGMD AELKSPAAIT SAALAGDPVA AAVLEQFCVF
     LGRVVGNNVL TLGSLGGVYI VGGVVPRFTE FFMNSGFKRA MGEKGVMSGY FKNLPVWLVT
     AEYPGLMGSG VALQQAFGSQ I
//
DBGET integrated database retrieval system