ID A0A060QBW8_9PROT Unreviewed; 178 AA.
AC A0A060QBW8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=ASAP_0370 {ECO:0000313|EMBL:CDG38415.1};
OS Asaia bogorensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Asaia.
OX NCBI_TaxID=91915 {ECO:0000313|EMBL:CDG38415.1, ECO:0000313|Proteomes:UP000027583};
RN [1] {ECO:0000313|EMBL:CDG38415.1, ECO:0000313|Proteomes:UP000027583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF2.1 {ECO:0000313|EMBL:CDG38415.1,
RC ECO:0000313|Proteomes:UP000027583};
RX PubMed=24682158; DOI=10.1093/gbe/evu062;
RA Chouaia B., Gaiarsa S., Crotti E., Comandatore F., Degli Esposti M.,
RA Ricci I., Alma A., Favia G., Bandi C., Daffonchio D.;
RT "Acetic acid bacteria genomes reveal functional traits for adaptation to
RT life in insect guts.";
RL Genome Biol. Evol. 6:912-920(2014).
RN [2] {ECO:0000313|EMBL:CDG38415.1, ECO:0000313|Proteomes:UP000027583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF2.1 {ECO:0000313|EMBL:CDG38415.1,
RC ECO:0000313|Proteomes:UP000027583};
RX PubMed=24804722; DOI=10.1371/journal.pone.0096566;
RA Degli Esposti M., Chouaia B., Comandatore F., Crotti E., Sassera D.,
RA Lievens P.M., Daffonchio D., Bandi C.;
RT "Evolution of mitochondria reconstructed from the energy metabolism of
RT living bacteria.";
RL PLoS ONE 9:e96566-e96566(2014).
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:CDG38415.1}.
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DR EMBL; CBLX010000003; CDG38415.1; -; Genomic_DNA.
DR RefSeq; WP_031240682.1; NZ_CBLX010000003.1.
DR AlphaFoldDB; A0A060QBW8; -.
DR eggNOG; COG3265; Bacteria.
DR Proteomes; UP000027583; 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; IPR031322; Shikimate/glucono_kinase.
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; PF01202; SKI; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363066}.
SQ SEQUENCE 178 AA; 19074 MW; 194BFCEFC0600BB9 CRC64;
MSAAHNPAAD RAAPGLFVVM GVSGCGKTTV AQGLADHFGW PFQEGDDLHP PANVAKMHSG
IPLDDSDRAP WLKICHEWLR DHAATGGVLT CSALKRKYRD TLRSGLNVTF VYLETSERTI
AERLKHRIGH FMPPSLLPSQ LATLEAPGPD ENVVTVDSAG TPEIVMAKLI ASLQSKAG
//
