ID Q63H40_BACCZ Unreviewed; 511 AA.
AC Q63H40;
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=Gluconokinase {ECO:0000313|EMBL:AAU20078.1};
DE EC=2.7.1.12 {ECO:0000313|EMBL:AAU20078.1};
GN Name=gntK {ECO:0000313|EMBL:AAU20078.1};
GN OrderedLocusNames=BCE33L0155 {ECO:0000313|EMBL:AAU20078.1};
OS Bacillus cereus (strain ZK / E33L).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=288681 {ECO:0000313|EMBL:AAU20078.1, 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; AAU20078.1; -; Genomic_DNA.
DR RefSeq; WP_000100549.1; NZ_CP009968.1.
DR AlphaFoldDB; Q63H40; -.
DR KEGG; bcz:BCE33L0155; -.
DR PATRIC; fig|288681.22.peg.5474; -.
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; PS00445; FGGY_KINASES_2; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|RuleBase:RU003733, ECO:0000313|EMBL:AAU20078.1};
KW Transferase {ECO:0000256|RuleBase:RU003733, ECO:0000313|EMBL:AAU20078.1}.
FT DOMAIN 4..246
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 256..451
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 511 AA; 56853 MW; F4A231F682FF8399 CRC64;
MSSYMLGIDI GTTSTKAVLF TEKGEVIQTE NIGYPLRTPD ISTAEQDPEE IFQAVLQAIS
NITKQHSDKN PSFISFSSAM HSVIAMDEND QPLTPCITWA DNRSEAWAHK IKDELNGHAV
YRRTGTPIHP MSPLSKITWI VNDHPEIAIR TKKYIGIKEY IFKKLFDQYV VDHSIASCMG
MMNLKTLDWD EEALKIAGIT SAQLSKLVPT TKIFSNCNPD LAQKIGIDSQ TPFVIGASDG
VLSNLGVNAI RKGEIAVTIG TSGAIRTIID KPQTDKKGRI FCYALTEKHW VIGGPVNNGG
MVLRWIRDEL ASSEVETAKR LGIDPYDVLT KIAERVRPGA DGLLFHPYLA GERAPLWNPD
VRGSFFGLTM SHKKEHMIRA ALEGVIYNLY TVFLALTECM DGPVTRIQAT GGFARSDVWR
QMMSDIFASE VVVPKSYESS CLGACILGLY ATGKIDSFEI VSEMVGSTYK HTPKEEATKE
YRQLLPIFIN LSRALEDDYT RIANYQRNLI K
//
