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GAL1_STRMU
ID   GAL1_STRMU              Reviewed;         390 AA.
AC   P96993;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2002, sequence version 2.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Galactokinase {ECO:0000255|HAMAP-Rule:MF_00246};
DE            EC=2.7.1.6 {ECO:0000255|HAMAP-Rule:MF_00246};
DE   AltName: Full=Galactose kinase {ECO:0000255|HAMAP-Rule:MF_00246};
GN   Name=galK {ECO:0000255|HAMAP-Rule:MF_00246}; OrderedLocusNames=SMU_886;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Ingbritt;
RX   PubMed=8973358; DOI=10.1016/s0378-1119(96)00434-9;
RA   Ajdic D., Sutcliffe I.C., Russell R.R.B., Ferretti J.J.;
RT   "Organization and nucleotide sequence of the Streptococcus mutans galactose
RT   operon.";
RL   Gene 180:137-144(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC   -!- FUNCTION: Catalyzes the transfer of the gamma-phosphate of ATP to D-
CC       galactose to form alpha-D-galactose-1-phosphate (Gal-1-P).
CC       {ECO:0000255|HAMAP-Rule:MF_00246}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-galactose + ATP = ADP + alpha-D-galactose 1-phosphate
CC         + H(+); Xref=Rhea:RHEA:13553, ChEBI:CHEBI:15378, ChEBI:CHEBI:28061,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58336, ChEBI:CHEBI:456216; EC=2.7.1.6;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00246};
CC   -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC       {ECO:0000255|HAMAP-Rule:MF_00246}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00246}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. GalK subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00246}.
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DR   EMBL; U21942; AAB49736.1; -; Genomic_DNA.
DR   EMBL; AE014133; AAN58600.1; -; Genomic_DNA.
DR   PIR; JC5311; JC5311.
DR   RefSeq; NP_721294.1; NC_004350.2.
DR   RefSeq; WP_002262879.1; NC_004350.2.
DR   AlphaFoldDB; P96993; -.
DR   SMR; P96993; -.
DR   STRING; 210007.SMU_886; -.
DR   PRIDE; P96993; -.
DR   EnsemblBacteria; AAN58600; AAN58600; SMU_886.
DR   KEGG; smu:SMU_886; -.
DR   PATRIC; fig|210007.7.peg.793; -.
DR   eggNOG; COG0153; Bacteria.
DR   HOGENOM; CLU_017814_2_1_9; -.
DR   OMA; PVCYNLR; -.
DR   PhylomeDB; P96993; -.
DR   UniPathway; UPA00214; -.
DR   Proteomes; UP000002512; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004335; F:galactokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006012; P:galactose metabolic process; IMP:CACAO.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.890; -; 1.
DR   HAMAP; MF_00246; Galactokinase; 1.
DR   InterPro; IPR000705; Galactokinase.
DR   InterPro; IPR022963; Galactokinase_bac.
DR   InterPro; IPR019741; Galactokinase_CS.
DR   InterPro; IPR019539; GalKase_N.
DR   InterPro; IPR013750; GHMP_kinase_C_dom.
DR   InterPro; IPR036554; GHMP_kinase_C_sf.
DR   InterPro; IPR006204; GHMP_kinase_N_dom.
DR   InterPro; IPR006203; GHMP_knse_ATP-bd_CS.
DR   InterPro; IPR006206; Mevalonate/galactokinase.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   PANTHER; PTHR10457:SF6; PTHR10457:SF6; 1.
DR   Pfam; PF10509; GalKase_gal_bdg; 1.
DR   Pfam; PF08544; GHMP_kinases_C; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   PIRSF; PIRSF000530; Galactokinase; 1.
DR   PRINTS; PR00473; GALCTOKINASE.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55060; SSF55060; 1.
DR   TIGRFAMs; TIGR00131; gal_kin; 1.
DR   PROSITE; PS00106; GALACTOKINASE; 1.
DR   PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Carbohydrate metabolism; Cytoplasm; Galactose metabolism;
KW   Kinase; Magnesium; Metal-binding; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..390
FT                   /note="Galactokinase"
FT                   /id="PRO_0000184627"
FT   ACT_SITE        174
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT   BINDING         33..36
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT   BINDING         67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT   BINDING         124..130
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT   BINDING         130
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT   BINDING         162
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT   BINDING         224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT   SITE            27
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00246"
FT   CONFLICT        95
FT                   /note="P -> A (in Ref. 1; AAB49736)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        246
FT                   /note="S -> T (in Ref. 1; AAB49736)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        339
FT                   /note="A -> S (in Ref. 1; AAB49736)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        374
FT                   /note="A -> R (in Ref. 1; AAB49736)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   390 AA;  43235 MW;  9DD2123A78BDA950 CRC64;
     MKKQELNQAF THVFGREADA TFFSPGRINL IGEHTDYNGG RVFPAAITLG TYGAARKRDD
     KLLRFYSANF EELGIIEISL DHLIFNKKDS WTNYPKGVIK YLQEAGHSID TGMDVYVFGN
     IPNGSGLSSS SSLELLIGIM AEELFDLKLD RLDLVKIGKR TENDFIGVNS GIMDQFAIGM
     GAEKKAIYLD TKTLEYDLVP LDLGDNVIVI MNTNKRRELA DSKYNERRTE CEKAVEELNV
     LLDIKSLGEL DEETFDEYAY LIKDAKRIKR ARHAVSENQR TLKAKKALAA GDLEKFGRLV
     NASHVSLEHD YEVTGIELDT LAHTAWEQEG VLGARMTGAG FGGCGIAIVA KDKVAALKEN
     VGRIYTETVG YAPAFYIAEI AGGSRVLSRK
 
 
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