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GLK_BURMA
ID   GLK_BURMA               Reviewed;         641 AA.
AC   Q62HW8;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Bifunctional protein glk;
DE   Includes:
DE     RecName: Full=Glucokinase;
DE              EC=2.7.1.2;
DE     AltName: Full=Glucose kinase;
DE   Includes:
DE     RecName: Full=Putative HTH-type transcriptional regulator;
GN   Name=glk; OrderedLocusNames=BMA2132;
OS   Burkholderia mallei (strain ATCC 23344).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=243160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23344;
RX   PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA   Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA   Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA   Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA   Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA   Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA   Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT   "Structural flexibility in the Burkholderia mallei genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
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: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the bacterial
CC       glucokinase family. {ECO:0000305}.
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DR   EMBL; CP000010; AAU49971.1; -; Genomic_DNA.
DR   RefSeq; WP_011204087.1; NC_006348.1.
DR   RefSeq; YP_103702.1; NC_006348.1.
DR   AlphaFoldDB; Q62HW8; -.
DR   SMR; Q62HW8; -.
DR   STRING; 243160.BMA2132; -.
DR   EnsemblBacteria; AAU49971; AAU49971; BMA2132.
DR   KEGG; bma:BMA2132; -.
DR   PATRIC; fig|243160.12.peg.2200; -.
DR   eggNOG; COG0837; Bacteria.
DR   eggNOG; COG1737; Bacteria.
DR   HOGENOM; CLU_016801_0_0_4; -.
DR   OMA; WSHVSFE; -.
DR   Proteomes; UP000006693; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
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; cd05013; SIS_RpiR; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   HAMAP; MF_00524; Glucokinase; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR003836; Glucokinase.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR000281; HTH_RpiR.
DR   InterPro; IPR035472; RpiR-like_SIS.
DR   InterPro; IPR001347; SIS_dom.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF02685; Glucokinase; 1.
DR   Pfam; PF01418; HTH_6; 1.
DR   Pfam; PF01380; SIS; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   SUPFAM; SSF53067; SSF53067; 1.
DR   SUPFAM; SSF53697; SSF53697; 1.
DR   TIGRFAMs; TIGR00749; glk; 1.
DR   PROSITE; PS51071; HTH_RPIR; 1.
DR   PROSITE; PS51464; SIS; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Glycolysis; Kinase; Membrane;
KW   Multifunctional enzyme; Nucleotide-binding; Transcription;
KW   Transcription regulation; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..641
FT                   /note="Bifunctional protein glk"
FT                   /id="PRO_0000268797"
FT   TRANSMEM        576..596
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          341..417
FT                   /note="HTH rpiR-type"
FT   DOMAIN          461..600
FT                   /note="SIS"
FT   DNA_BIND        377..396
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250"
FT   REGION          1..340
FT                   /note="Glucokinase"
FT   REGION          341..641
FT                   /note="Putative HTH-type transcriptional regulator"
FT   BINDING         23..28
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   641 AA;  68376 MW;  65D23DA89E0AD2EA CRC64;
     MSTGAQTKAA AASQHADGPR LLADVGGTNA RFALETGPGE ITQIRVYPGA EYPTLTDAIR
     KYLKDAKIGR VNHAAIAIAN PVDGDQVRMT NHNWSFSIEA TRRALGFDTL LVVNDFTALA
     MALPGLTDAQ RVQIGGGTRR QNSVIGLMGP GTGLGVSGLI PADDRWIALG SEGGHATFAP
     MDEREDLVLQ YARRKYPHVS FERVCAGPGM EIIYRALAAR DKKRIAANVD TADIVERAHA
     GDALALEAVE CFCAILGTFA GNLAVTLGAL GGIYIGGGVV PKLGELFMRS PFRARFEAKG
     RFEAYLANIP TYLITAEYPA FLGVSAILAE QLSNRTGGAS SAVFERIRQM RDALTPAERR
     VADLALNHPR SIINDPIVNI ARKADVSQPT VIRFCRSLGC QGLSDFKLKL ATGLTGTIPM
     SHSQVHLGDT ATDFGAKVLD NTVSAILQLR EHLNFEHVEQ AIDILNNARR IEFYGLGNSN
     IVAQDAHYKF FRFGIPTIAY GDLYMQAASA ALLGKGDVIV AVSKSGRAPE LLRVLDVAMQ
     AGAKVIAITS SNTPLAKRAT VALETDHIEM RESQLSMISR ILHLVMIDIL AVGVAIRRAA
     PNAELAEAMA RAKARAGASA GDEAADVLDW LSHGAAPAAK D
 
 
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