ID Q638K2_BACCZ Unreviewed; 513 AA.
AC Q638K2;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Gluconate kinase (2-dehydro-3-deoxygluconokinase) {ECO:0000313|EMBL:AAU17182.1};
DE EC=2.7.1.12 {ECO:0000313|EMBL:AAU17182.1};
GN Name=gntK {ECO:0000313|EMBL:AAU17182.1};
GN OrderedLocusNames=BCE33L3078 {ECO:0000313|EMBL:AAU17182.1};
OS Bacillus cereus (strain ZK / E33L).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=288681 {ECO:0000313|EMBL:AAU17182.1, ECO:0000313|Proteomes:UP000002612};
RN [1] {ECO:0000313|Proteomes:UP000002612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZK / E33L {ECO:0000313|Proteomes:UP000002612};
RX PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Brown N.,
RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Green L.D., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T.,
RA Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E.,
RA Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Ticknor L.O., Wills P.L., Brettin T.S., Gilna P.;
RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT thuringiensis isolates closely related to Bacillus anthracis.";
RL J. Bacteriol. 188:3382-3390(2006).
CC -!- SIMILARITY: Belongs to the FGGY kinase family.
CC {ECO:0000256|RuleBase:RU003733}.
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DR EMBL; CP000001; AAU17182.1; -; Genomic_DNA.
DR RefSeq; WP_000252451.1; NZ_CP009968.1.
DR AlphaFoldDB; Q638K2; -.
DR KEGG; bcz:BCE33L3078; -.
DR PATRIC; fig|288681.22.peg.2363; -.
DR Proteomes; UP000002612; Chromosome.
DR GO; GO:0046316; F:gluconokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0019521; P:D-gluconate 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 InterPro; IPR006002; Gluconate_kinase.
DR NCBIfam; TIGR01314; gntK_FGGY; 1.
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; PS00933; FGGY_KINASES_1; 1.
DR PROSITE; PS00445; FGGY_KINASES_2; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|RuleBase:RU003733, ECO:0000313|EMBL:AAU17182.1};
KW Transferase {ECO:0000256|RuleBase:RU003733, ECO:0000313|EMBL:AAU17182.1}.
FT DOMAIN 6..250
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 260..454
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 513 AA; 56979 MW; 8FBDCB163766A9F1 CRC64;
MVRSKYMIGV DIGTTSTKSV LFSTDGSVIA SHGIEYPLYS PTPETAEQDP EEIFRAVIHT
IKETVQSSSV QPNDILCVSF SSAMHSIIAV DEKGKPLTRC ITWADNRSAS WAEKIKNDMN
GHEIYLRTGT PIHPMSPLSK LVWLQNEQAE LFAKTYKFIS IKEYVFYKLY KEYVIDYSIA
SATGMFNLKS LKWDEEALYV AGITDDKLSK LVPTTHSLTG LDEELANEMN VLVSTPFVVG
ASDGVLSNLG VNAIDPGVVA VTIGTSGAIR AVTNRPVTDP KGRIFCYALT EDHWVIGGPV
NNGGMIFRWA RDQLGTSEIE LAKRLGKDPY EVLTEIAAKV NPGSDGLLFH PYLAGERAPL
WNANARGSFF GLGLHHKKEH LIRAVLEGVI YNLYTVLLAL KELIGEPKKI QATGGFARSE
LWRQMMADIF HQDVYVPESF ESSCLGAAIL GLYSLGEVDT LHVVSEMVGA NFHHEPNMES
VEKYKDLTPI YIRLSRQLEE EYESIAAYQK KWV
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