ID A0A261G8A5_9BIFI Unreviewed; 227 AA.
AC A0A261G8A5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Gluconokinase {ECO:0000256|ARBA:ARBA00012054, ECO:0000256|RuleBase:RU363066};
DE EC=2.7.1.12 {ECO:0000256|ARBA:ARBA00012054, ECO:0000256|RuleBase:RU363066};
GN ORFNames=BAQU_1309 {ECO:0000313|EMBL:OZG67236.1};
OS Bifidobacterium aquikefiri.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1653207 {ECO:0000313|EMBL:OZG67236.1, ECO:0000313|Proteomes:UP000216451};
RN [1] {ECO:0000313|EMBL:OZG67236.1, ECO:0000313|Proteomes:UP000216451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 28769 {ECO:0000313|EMBL:OZG67236.1,
RC ECO:0000313|Proteomes:UP000216451};
RX PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA van Sinderen D., Ventura M.;
RT "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT family.";
RL BMC Genomics 18:568-568(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+);
CC Xref=Rhea:RHEA:19433, ChEBI:CHEBI:15378, ChEBI:CHEBI:18391,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58759, ChEBI:CHEBI:456216;
CC EC=2.7.1.12; Evidence={ECO:0000256|ARBA:ARBA00001329,
CC ECO:0000256|RuleBase:RU363066};
CC -!- PATHWAY: Carbohydrate acid metabolism; D-gluconate degradation.
CC {ECO:0000256|ARBA:ARBA00004875}.
CC -!- SIMILARITY: Belongs to the gluconokinase GntK/GntV family.
CC {ECO:0000256|ARBA:ARBA00008420, ECO:0000256|RuleBase:RU363066}.
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:OZG67236.1}.
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DR EMBL; MWXA01000005; OZG67236.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261G8A5; -.
DR Proteomes; UP000216451; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046316; F:gluconokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd02021; GntK; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006001; Therm_gnt_kin.
DR NCBIfam; TIGR01313; therm_gnt_kin; 1.
DR PANTHER; PTHR43442; GLUCONOKINASE-RELATED; 1.
DR PANTHER; PTHR43442:SF3; GLUCONOKINASE-RELATED; 1.
DR Pfam; PF13671; AAA_33; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363066};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU363066};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363066};
KW Reference proteome {ECO:0000313|Proteomes:UP000216451};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363066}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 227 AA; 25136 MW; 90969CE54EBDC271 CRC64;
MLSTKRQTHY GASSTSTATK QKARILMSDT QEQLSKPIHI VVMGVAGSGK STVAEALRDR
LGLTMAEGDD FHPQANIDKM SQGIPLTDAD RRPWLEVINR WMLGRNALGE STVVSSSALK
RSYRDILRKD VPVFFVHLVG SQELIQRRLS ERKGHFMPPA LLPSQFADLE PLQPDEPGIE
VSVEGTSEEM IQRSIDAVKA HAEREESQTS EAIADKADES LKSSNER
//
