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GLK_ECO57
ID   GLK_ECO57               Reviewed;         321 AA.
AC   P0A6V9; P46880; P78276;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Glucokinase;
DE            EC=2.7.1.2;
DE   AltName: Full=Glucose kinase;
GN   Name=glk; OrderedLocusNames=Z3654, ECs3268;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX   PubMed=15466045; DOI=10.1128/jb.186.20.6915-6927.2004;
RA   Lunin V.V., Li Y., Schrag J.D., Iannuzzi P., Cygler M., Matte A.;
RT   "Crystal structures of Escherichia coli ATP-dependent glucokinase and its
RT   complex with glucose.";
RL   J. Bacteriol. 186:6915-6927(2004).
CC   -!- FUNCTION: Not highly important in E.coli as glucose is transported into
CC       the cell by the PTS system already as glucose 6-phosphate.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the bacterial glucokinase family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG57514.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB36691.1; -; Genomic_DNA.
DR   PIR; D91037; D91037.
DR   PIR; F85881; F85881.
DR   RefSeq; NP_311295.1; NC_002695.1.
DR   RefSeq; WP_000170346.1; NZ_SWKA01000005.1.
DR   PDB; 1Q18; X-ray; 2.36 A; A/B=2-321.
DR   PDB; 1SZ2; X-ray; 2.20 A; A/B=2-321.
DR   PDBsum; 1Q18; -.
DR   PDBsum; 1SZ2; -.
DR   AlphaFoldDB; P0A6V9; -.
DR   SMR; P0A6V9; -.
DR   STRING; 155864.EDL933_3557; -.
DR   EnsemblBacteria; AAG57514; AAG57514; Z3654.
DR   EnsemblBacteria; BAB36691; BAB36691; ECs_3268.
DR   GeneID; 915629; -.
DR   KEGG; ece:Z3654; -.
DR   KEGG; ecs:ECs_3268; -.
DR   PATRIC; fig|386585.9.peg.3412; -.
DR   eggNOG; COG0837; Bacteria.
DR   HOGENOM; CLU_042582_1_0_6; -.
DR   OMA; NNHWRLS; -.
DR   BRENDA; 2.7.1.2; 2026.
DR   EvolutionaryTrace; P0A6V9; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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   HAMAP; MF_00524; Glucokinase; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR003836; Glucokinase.
DR   Pfam; PF02685; Glucokinase; 1.
DR   SUPFAM; SSF53067; SSF53067; 1.
DR   TIGRFAMs; TIGR00749; glk; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; Glycolysis; Kinase;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..321
FT                   /note="Glucokinase"
FT                   /id="PRO_0000215125"
FT   BINDING         8..13
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   STRAND          4..11
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   STRAND          14..21
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   TURN            22..24
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   STRAND          27..34
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   HELIX           35..37
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   HELIX           41..51
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   STRAND          58..65
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   STRAND          69..72
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   STRAND          75..77
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   HELIX           83..90
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   STRAND          93..99
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   HELIX           100..107
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   HELIX           108..110
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   HELIX           113..115
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   STRAND          116..118
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   STRAND          130..147
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   STRAND          150..155
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   HELIX           158..160
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   HELIX           168..180
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   STRAND          181..183
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   HELIX           186..188
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   HELIX           192..205
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   HELIX           215..224
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   HELIX           228..252
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   STRAND          257..261
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   STRAND          263..265
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   HELIX           266..268
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   HELIX           269..274
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   HELIX           277..282
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   HELIX           285..287
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   HELIX           288..291
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   STRAND          296..299
FT                   /evidence="ECO:0007829|PDB:1SZ2"
FT   HELIX           304..316
FT                   /evidence="ECO:0007829|PDB:1SZ2"
SQ   SEQUENCE   321 AA;  34723 MW;  2D6CD956641A3823 CRC64;
     MTKYALVGDV GGTNARLALC DIASGEISQA KTYSGLDYPS LEAVIRVYLE EHKVEVKDGC
     IAIACPITGD WVAMTNHTWA FSIAEMKKNL GFSHLEIIND FTAVSMAIPM LKKEHLIQFG
     GAEPVEGKPI AVYGAGTGLG VAHLVHVDKR WVSLPGEGGH VDFAPNSEEE AIILEILRAE
     IGHVSAERVL SGPGLVNLYR AIVKADNRLP ENLKPKDITE RALADSCTDC RRALSLFCVI
     MGRFGGNLAL NLGTFGGVFI AGGIVPRFLE FFKASGFRAA FEDKGRFKEY VHDIPVYLIV
     HDNPGLLGSG AHLRQTLGHI L
 
 
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