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Database: UniProt
Entry: L0A1M1_DEIPD
LinkDB: L0A1M1_DEIPD
Original site: L0A1M1_DEIPD 
ID   L0A1M1_DEIPD            Unreviewed;       497 AA.
AC   L0A1M1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Pentulose/hexulose kinase {ECO:0000313|EMBL:AFZ66910.1};
GN   OrderedLocusNames=Deipe_1361 {ECO:0000313|EMBL:AFZ66910.1};
OS   Deinococcus peraridilitoris (strain DSM 19664 / LMG 22246 / CIP 109416 /
OS   KR-200).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=937777 {ECO:0000313|EMBL:AFZ66910.1, ECO:0000313|Proteomes:UP000010467};
RN   [1] {ECO:0000313|Proteomes:UP000010467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19664 / LMG 22246 / CIP 109416 / KR-200
RC   {ECO:0000313|Proteomes:UP000010467};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Lu M.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Pukall R., Steenblock K., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "Complete sequence of chromosome of Deinococcus peraridilitoris DSM
RT   19664.";
RL   Submitted (MAR-2012) 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; CP003382; AFZ66910.1; -; Genomic_DNA.
DR   RefSeq; WP_015235218.1; NC_019793.1.
DR   AlphaFoldDB; L0A1M1; -.
DR   STRING; 937777.Deipe_1361; -.
DR   KEGG; dpd:Deipe_1361; -.
DR   PATRIC; fig|937777.3.peg.1366; -.
DR   eggNOG; COG1070; Bacteria.
DR   HOGENOM; CLU_009281_3_3_0; -.
DR   OrthoDB; 9805576at2; -.
DR   Proteomes; UP000010467; 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; cd07804; FGGY_XK_like_1; 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; SUGAR KINASE; 1.
DR   PANTHER; PTHR43095:SF5; XYLULOSE 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:AFZ66910.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010467};
KW   Transferase {ECO:0000256|RuleBase:RU003733}.
FT   DOMAIN          5..248
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          259..445
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
SQ   SEQUENCE   497 AA;  54082 MW;  BF27C4C9037BB7B5 CRC64;
     MSDLLLGIDV GTYSSKGVLV TPAGQILKSH VVPHGIDMPQ PGHVEQDADN VWWQDVVQII
     RELLNGEPYS GADVAGIAVS AIGPCLLALD EHGRPLRPGI LYGVDTRAHA EVAELEREYG
     EAGILERSLM SFTSQAIGPK IRWLQRHEGS VWQQTRTLTT ASSYLAFRLT GEHVMDRHTA
     SHYMPLYDPR KHGWNEALAD EFLGNVRLPR LGWSDSPLGT VTSRAAAQTG LREGTPVAVG
     AVDALSEAIS VGAVRSGDLM IMYGSTTFFI LVQDVPTPDT RVWTVSGAFE GQYNLAAGMS
     TTGSLTRWFR DEFARDLPEE RAYDELFQAA QNIPPGAGGL LVLPYFSGER TPINDTKAKG
     IIAGLTLSHS REHVFRAVLE SVGFGIRHNL ETFRALGADI KRVIAVGGGT KSQTWLQIVS
     DIAGVTQLVP AKTIGASYGD AFLAGLVTGN VTRDALMHWV GEAQEVTPNP TTTEVYDHQY
     QAYRQLYLQT RSVIHSL
//
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