ID C1D2H4_DEIDV Unreviewed; 485 AA.
AC C1D2H4;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Putative carbohydrate kinase {ECO:0000313|EMBL:ACO47613.1};
GN OrderedLocusNames=Deide_1p01630 {ECO:0000313|EMBL:ACO47613.1};
OS Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OG Plasmid pDeide1 {ECO:0000313|Proteomes:UP000002208}.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO47613.1, ECO:0000313|Proteomes:UP000002208};
RN [1] {ECO:0000313|EMBL:ACO47613.1, ECO:0000313|Proteomes:UP000002208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115
RC {ECO:0000313|Proteomes:UP000002208};
RC PLASMID=pDeide1 {ECO:0000313|Proteomes:UP000002208};
RX PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT bacterium Deinococcus deserti.";
RL PLoS Genet. 5:E1000434-E1000434(2009).
CC -!- SIMILARITY: Belongs to the FGGY kinase family.
CC {ECO:0000256|RuleBase:RU003733}.
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DR EMBL; CP001115; ACO47613.1; -; Genomic_DNA.
DR AlphaFoldDB; C1D2H4; -.
DR KEGG; ddr:Deide_1p01630; -.
DR HOGENOM; CLU_009281_3_2_0; -.
DR OrthoDB; 9805576at2; -.
DR Proteomes; UP000002208; Plasmid pDeide1.
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:ACO47613.1};
KW Plasmid {ECO:0000313|EMBL:ACO47613.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002208};
KW Transferase {ECO:0000256|RuleBase:RU003733}.
FT DOMAIN 11..247
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 286..438
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 485 AA; 51639 MW; 8DDC310EF4AB15A9 CRC64;
MRAVHAPPPV VLALDLGSSS VKGAAFDIHG RVLAGLEAHE NVSLHYAAGG AAEVPLADLV
AAAEAVLDRL HGRLGSRSVL AVAMTSIASS LVALDARGEP VGPVLSYADT RSAGEVRAVE
TLTSREETGC PAFSAYWPAQ VRWWQGAHPE LPAEHFCSVP DFLLMRWTGE LVTSYSLASW
TGLLDRETLD WNMRALSTAG LSAAQLPRLG DHDTRLTLQS RWTDRWPKLA GVPFHPGVAD
GATANVGSGA LTPGRPAITI GSTSAVRLAV QGAPPPIPSG LWSYRIDRNT HLLGGALTEG
GNLYSWLQST LRLDRRLDEE LLGMAPGAHG LTFVPSLGGT RSPDYDPHAR GTLHGLSYAT
TPAQITRAAM EGVACRLANV AWRLPVSDDA LFVASGRALL ASRAWPQMLA DALGRPLLLE
DIRAGASARG AALLALRAQG VEISTDPVAQ RVVEPVPAHH EVYRTMCARM DRLTRLMRED
EELVS
//
