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Database: UniProt
Entry: A0A235HTI2_9NOSO
LinkDB: A0A235HTI2_9NOSO
Original site: A0A235HTI2_9NOSO 
ID   A0A235HTI2_9NOSO        Unreviewed;       341 AA.
AC   A0A235HTI2;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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   ORFNames=CDG77_23380 {ECO:0000313|EMBL:OYD88475.1};
OS   Nostoc sp. 'Peltigera membranacea cyanobiont' 213.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=2014530 {ECO:0000313|EMBL:OYD88475.1, ECO:0000313|Proteomes:UP000215421};
RN   [1] {ECO:0000313|EMBL:OYD88475.1, ECO:0000313|Proteomes:UP000215421}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=213 {ECO:0000313|EMBL:OYD88475.1,
RC   ECO:0000313|Proteomes:UP000215421};
RA   Gagunashvili A.N., Andresson O.S.;
RT   "Distinctive characters of Nostoc genomes in cyanolichens.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OYD88475.1}.
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DR   EMBL; NOLI01000100; OYD88475.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A235HTI2; -.
DR   Proteomes; UP000215421; Unassembled WGS sequence.
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   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; PTHR47363; GLUCOKINASE; 1.
DR   PANTHER; PTHR47363: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, ECO:0000313|EMBL:OYD88475.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00524};
KW   Transferase {ECO:0000256|HAMAP-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   341 AA;  37125 MW;  1E59F439563F8CCB CRC64;
     MTLLLAGDIG GTKTILRLVE TSDSPALHPI YQESYHSADF PDLVPIVQKF LVKANTPIPE
     KACFAIAGPI VKNTAKLTNL AWFLDTERLQ EELGIPHISL INDFAAIGYG ISGLQEQDLL
     TLQVGKSQPE APIGIIGAGT GLGQGFLIKQ GNDYQVFPSE GGHADFAPRN EIEFQLLRYL
     LGKHDIQRLS VERVVSGMGI VAIYQFLRDR KFATESPDIA RIVRTWEQEA GQEEKSVDPG
     AVIGTAALEG RDRLSEQTLQ LFIEAYGAEA GNLALKLLPY GGLYIAGGIA PKILPLIQNN
     GFLLNFTQKG RMRRLLEEIP VYIILNPQVG LIGAALCAAR L
//
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