ID A0A1G0WCL7_9BACT Unreviewed; 485 AA.
AC A0A1G0WCL7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Phosphotransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2X47_04440 {ECO:0000313|EMBL:OGV18938.1};
OS Lentisphaerae bacterium GWF2_38_69.
OC Bacteria; Lentisphaerota.
OX NCBI_TaxID=1798570 {ECO:0000313|EMBL:OGV18938.1, ECO:0000313|Proteomes:UP000176746};
RN [1] {ECO:0000313|EMBL:OGV18938.1, ECO:0000313|Proteomes:UP000176746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:16125, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:37721, ChEBI:CHEBI:61527, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001397};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126;
CC Evidence={ECO:0000256|ARBA:ARBA00001397};
CC -!- PATHWAY: Carbohydrate degradation. {ECO:0000256|ARBA:ARBA00004921}.
CC -!- PATHWAY: Carbohydrate metabolism. {ECO:0000256|ARBA:ARBA00005007}.
CC -!- SIMILARITY: Belongs to the hexokinase family.
CC {ECO:0000256|ARBA:ARBA00009225}.
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:OGV18938.1}.
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DR EMBL; MHBE01000040; OGV18938.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0WCL7; -.
DR STRING; 1798570.A2X47_04440; -.
DR UniPathway; UPA00109; UER00180.
DR Proteomes; UP000176746; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR GO; GO:0004396; F:hexokinase activity; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0001678; P:intracellular glucose homeostasis; IEA:InterPro.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 1.
DR Gene3D; 3.40.367.20; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR001312; Hexokinase.
DR InterPro; IPR022673; Hexokinase_C.
DR InterPro; IPR022672; Hexokinase_N.
DR PANTHER; PTHR19443; HEXOKINASE; 1.
DR PANTHER; PTHR19443:SF16; HEXOKINASE TYPE 1-RELATED; 1.
DR Pfam; PF00349; Hexokinase_1; 1.
DR Pfam; PF03727; Hexokinase_2; 1.
DR PRINTS; PR00475; HEXOKINASE.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR PROSITE; PS51748; HEXOKINASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..485
FT /note="Phosphotransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009568859"
FT DOMAIN 47..239
FT /note="Hexokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00349"
FT DOMAIN 246..479
FT /note="Hexokinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03727"
SQ SEQUENCE 485 AA; 53919 MW; F9912FE41D96ADC4 CRC64;
MKKILILLLL FLLSADLLAN NSQVEPRGSN YDLYSSRSST ADEDFIRYIE KNFAVTPDDI
REIIANFHSE MRKGLSGQES SLQMIPSFTD VAIGKETGKF IALDLGGTNL RVLAVDLDGA
KGIEISGVNR YVIEKKYMEG TGEELFNYIA ECIDNFMKSN NISYEKKVDL AFTFSFAVDQ
TSIDSGKLIS WSKGFEASGV EGKDVVALLN EALRRKGIKN IKVAALVNDT VGTLVAKSYE
EQACDLGVIL GTGTNACYRE KINNIKKWKG LAPKSSNMII NMEWGDFDKI SVTYYDREMD
AGTINPKEHK FEKMISGMYL GEIFRLVLRD LIKRDIIFKD ENAVNLFDKQ WSLKSEFMSL
AANDKSSNLG AIEVFLSEQG LKKSDLQSRI LFKYISSLIA RRSARLSAAA VSAVILWMDP
ELERKHIVGI DGAVYERYPD YKGIMESVFN ELFGDKSKNI VCDYAKDGSG IGAAIIAAVV
ASEEG
//
