GenomeNet

Database: UniProt
Entry: U0EA32_9NOCA
LinkDB: U0EA32_9NOCA
Original site: U0EA32_9NOCA 
ID   U0EA32_9NOCA            Unreviewed;       176 AA.
AC   U0EA32;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
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=N806_03505 {ECO:0000313|EMBL:ERB50258.1};
OS   Rhodococcus sp. P27.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1384060 {ECO:0000313|EMBL:ERB50258.1, ECO:0000313|Proteomes:UP000016008};
RN   [1] {ECO:0000313|EMBL:ERB50258.1, ECO:0000313|Proteomes:UP000016008}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P27 {ECO:0000313|EMBL:ERB50258.1,
RC   ECO:0000313|Proteomes:UP000016008};
RX   PubMed=24072865;
RA   Gouvea Taketani R., Domingues Zucchi T., Soares de Melo I., Mendes R.;
RT   "Whole-Genome Shotgun Sequencing of Rhodococcus erythropolis Strain P27, a
RT   Highly Radiation-Resistant Actinomycete from Antarctica.";
RL   Genome Announc. 1:e00763-13(2013).
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:ERB50258.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AVCO01000053; ERB50258.1; -; Genomic_DNA.
DR   AlphaFoldDB; U0EA32; -.
DR   PATRIC; fig|1384060.5.peg.5983; -.
DR   Proteomes; UP000016008; 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   176 AA;  19249 MW;  FF1871BE279A550A CRC64;
     MNSEAAQQKQ YPVLVLMGVS GSGKSTVGGM LAGAMGWDLQ EGDDLHPQAN IDKMATGHPL
     NDDDRWPWLD KIAVWIKSHT DAGQPGIVTC SALKRSYRDV LRGEHVVFVH LAGSRDQIGQ
     RLTARLDHYM PASLLDSQIS TLEAVDPDEQ AIVVDVGGSP AKIAEEILRR VETFEY
//
DBGET integrated database retrieval system