ID B9KBK9_THENN Unreviewed; 476 AA.
AC B9KBK9;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Gluconate kinase {ECO:0000313|EMBL:ACM22405.1};
GN OrderedLocusNames=CTN_0229 {ECO:0000313|EMBL:ACM22405.1};
OS Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Thermotoga.
OX NCBI_TaxID=309803 {ECO:0000313|EMBL:ACM22405.1, ECO:0000313|Proteomes:UP000000445};
RN [1] {ECO:0000313|Proteomes:UP000000445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E
RC {ECO:0000313|Proteomes:UP000000445};
RA Lim S.K., Kim J.S., Cha S.H., Park B.C., Lee D.S., Tae H.S., Kim S.-J.,
RA Kim J.J., Park K.J., Lee S.Y.;
RT "The genome sequence of the hyperthermophilic bacterium Thermotoga
RT neapolitana.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACM22405.1, ECO:0000313|Proteomes:UP000000445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E
RC {ECO:0000313|Proteomes:UP000000445};
RX PubMed=19129632; DOI=10.1271/bbb.80567;
RA Lee D., Seo H., Park C., Park K.;
RT "WeGAS: a web-based microbial genome annotation system.";
RL Biosci. Biotechnol. Biochem. 73:213-216(2009).
CC -!- SIMILARITY: Belongs to the FGGY kinase family.
CC {ECO:0000256|RuleBase:RU003733}.
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DR EMBL; CP000916; ACM22405.1; -; Genomic_DNA.
DR RefSeq; WP_015918741.1; NC_011978.1.
DR AlphaFoldDB; B9KBK9; -.
DR STRING; 309803.CTN_0229; -.
DR KEGG; tna:CTN_0229; -.
DR eggNOG; COG1070; Bacteria.
DR HOGENOM; CLU_009281_3_2_0; -.
DR Proteomes; UP000000445; Chromosome.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd07770; FGGY_GntK; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000577; Carb_kinase_FGGY.
DR InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR InterPro; IPR018485; FGGY_C.
DR InterPro; IPR018484; FGGY_N.
DR PANTHER; PTHR43095:SF2; GLUCONOKINASE; 1.
DR PANTHER; PTHR43095; SUGAR KINASE; 1.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR PIRSF; PIRSF000538; GlpK; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR PROSITE; PS00445; FGGY_KINASES_2; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|RuleBase:RU003733, ECO:0000313|EMBL:ACM22405.1};
KW Transferase {ECO:0000256|RuleBase:RU003733}.
FT DOMAIN 1..231
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 241..425
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 476 AA; 54058 MW; E71E7020498F6DD8 CRC64;
MIAAIDIGTE SARLMFKSNG EWKVLKKSYR IFFPSPEAVE QDPEEILSAV YYLLKQIPKE
GDVLYVGMSS VFHSVVGLDE DFNPVTPLLN WVDRRSYREK EELEKKYGTR FFYERTACPL
HPMYWPSKIL WMKKNSDSKK FCSIKAFIVN KLTGEFVEEL SLASGTGMMN IHSLEWDDEI
LGIVGVKKEN LPELKSPYAQ LKAKEEVAKE LGFREVYLVL GGGDGVMTNV GLNAMDPNSA
TVTIGTSGAF RVVLDRPVID REGISTWCYL IDEKNYVLGG AINNGGIVLM WLKDVMKFDS
YDEIIEEAKK SSIGANGLVF LPFLNGERAP HWRERYRGVL VGLASSHRRS DIARAALEGI
CFRIKDIYNA VKKVGNVDPV RIVATGGFTS SPYWVQLLAD VLGKDITVTN VENPSAFGAY
VMALKSLGES VEEFLEKEVH VEQVFRCDPE RNEKYEQLYD DYRFLYEKLV DYFYRE
//