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Database: UniProt
Entry: A0A0H4P488_9BACI
LinkDB: A0A0H4P488_9BACI
Original site: A0A0H4P488_9BACI 
ID   A0A0H4P488_9BACI        Unreviewed;       512 AA.
AC   A0A0H4P488;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Gluconokinase {ECO:0000313|EMBL:AKP48951.1};
DE            EC=2.7.1.12 {ECO:0000313|EMBL:AKP48951.1};
GN   ORFNames=BSM4216_3801 {ECO:0000313|EMBL:AKP48951.1};
OS   Bacillus smithii.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1479 {ECO:0000313|EMBL:AKP48951.1, ECO:0000313|Proteomes:UP000036353};
RN   [1] {ECO:0000313|EMBL:AKP48951.1, ECO:0000313|Proteomes:UP000036353}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4216 {ECO:0000313|EMBL:AKP48951.1,
RC   ECO:0000313|Proteomes:UP000036353};
RA   Bosma E.F., Koehorst J.J., van Hijum S.A.F.T., Renckens B., Vriesendorp B.,
RA   van de Weijer A.H.P., Schaap P.J., de Vos W.M., van der Oost J.,
RA   van Kranenburg R.;
RT   "Complete genome sequence of thermophilic Bacillus smithii type strain DSM
RT   4216T.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family.
CC       {ECO:0000256|RuleBase:RU003733}.
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DR   EMBL; CP012024; AKP48951.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H4P488; -.
DR   STRING; 1479.BSM4216_3801; -.
DR   KEGG; bsm:BSM4216_3801; -.
DR   eggNOG; COG1070; Bacteria.
DR   OrthoDB; 9805576at2; -.
DR   Proteomes; UP000036353; 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:AKP48951.1};
KW   Transferase {ECO:0000256|RuleBase:RU003733, ECO:0000313|EMBL:AKP48951.1}.
FT   DOMAIN          5..249
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          259..453
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
SQ   SEQUENCE   512 AA;  57111 MW;  10BC8EDF638ACD66 CRC64;
     MSSKYVIGVD IGTTSTKSVL FSAEGSVISR HGIEYSLFSP TPETAEQDPE EIFRAVVNTI
     KRTIQDSHVQ PSDILCVSFS SAMHSVIAVD KEGKPLTNCI TWADNRSAKW AEKIKKEMNG
     HEIYRRTGTP IHPMSPLSKL TWLRNEHPEI FARSYKFISI KEYIFYKLFK EYVIDYSIAS
     ATGMFHLNSL KWDEEALHIA GISEEQLSRP VPTTYRLTGL DETFAKEMNL HPSTPFVVGA
     SDGVLSNLGV NAIDPGVVAV TIGTSGAIRT VTNRPVTDPK ERIFCYALTE NHWVIGGPVN
     NGGMIFRWVR DQLGSSEVET AKRLGKDPYE VLTEIAAKVN PGSDGLLFHP YLAGERAPLW
     DANARGSFFG LGLHHKKEHL IRAVLEGVIF NLYTVLLALE ELIGEPKKIQ ATGGFARSPL
     WRQMMADIFD QEVYIPESFE SSCLGAAILG LYSLGEIHSL HVVSEMVGAT HHHVPNPEHV
     SVYKELIPIY IRLSRLLKEE YESIAAFQKK RV
//
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