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Database: UniProt
Entry: A0A1E7ZEF4_9ALTE
LinkDB: A0A1E7ZEF4_9ALTE
Original site: A0A1E7ZEF4_9ALTE 
ID   A0A1E7ZEF4_9ALTE        Unreviewed;       317 AA.
AC   A0A1E7ZEF4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=BFC18_06875 {ECO:0000313|EMBL:OFC71870.1};
OS   Alteromonas confluentis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=1656094 {ECO:0000313|EMBL:OFC71870.1, ECO:0000313|Proteomes:UP000175691};
RN   [1] {ECO:0000313|EMBL:OFC71870.1, ECO:0000313|Proteomes:UP000175691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 42603 {ECO:0000313|EMBL:OFC71870.1,
RC   ECO:0000313|Proteomes:UP000175691};
RA   Seilhamer J.J.;
RL   Submitted (AUG-2016) 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:OFC71870.1}.
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DR   EMBL; MDHN01000010; OFC71870.1; -; Genomic_DNA.
DR   RefSeq; WP_070124244.1; NZ_MDHN01000010.1.
DR   AlphaFoldDB; A0A1E7ZEF4; -.
DR   STRING; 1656094.BFC18_06875; -.
DR   OrthoDB; 9800595at2; -.
DR   Proteomes; UP000175691; 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; 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, ECO:0000313|EMBL:OFC71870.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00524};
KW   Reference proteome {ECO:0000313|Proteomes:UP000175691};
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   317 AA;  34336 MW;  2897FE4F2FA75967 CRC64;
     MTEKFVADVG GTNIRLARVT ETGVDNIIKY QCKDFGSIDL AIEQYFKDLP DFTFTAGCIA
     IACPVLGDQV VMTNHSWAFS QKALKQQLDL EQLFVINDFT AVAHSLPVLG KDQVVQIGEG
     TPKENGNIAV FGPGTGLGVE HLTMTISGWQ TLDGEGGHVD FAPVDETDVI VWRYLQNQFA
     RASAEEVMSG RGLMNVYKAL AENANEPLAA NEPAEVTQKA LSGECHTCVR ALTQFCRIMG
     SFAGNLALNM ATTGGVFIGG GIANRFAEFL QDSDFRARFE AKGQMKLYVK DIPTYLIAEP
     DHGLLGASAY LKQHTAS
//
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