ID C1D3M0_DEIDV Unreviewed; 497 AA.
AC C1D3M0;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Putative rhamnulokinase {ECO:0000313|EMBL:ACO48099.1};
GN Name=rhaB {ECO:0000313|EMBL:ACO48099.1};
GN OrderedLocusNames=Deide_3p01560 {ECO:0000313|EMBL:ACO48099.1};
OS Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OG Plasmid pDeide3 {ECO:0000313|Proteomes:UP000002208}.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO48099.1, ECO:0000313|Proteomes:UP000002208};
RN [1] {ECO:0000313|EMBL:ACO48099.1, 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=pDeide3 {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|ARBA:ARBA00009156}.
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DR EMBL; CP001117; ACO48099.1; -; Genomic_DNA.
DR AlphaFoldDB; C1D3M0; -.
DR KEGG; ddr:Deide_3p01560; -.
DR HOGENOM; CLU_039395_0_1_0; -.
DR OrthoDB; 9761504at2; -.
DR Proteomes; UP000002208; Plasmid pDeide3.
DR GO; GO:0008993; F:rhamnulokinase activity; IEA:InterPro.
DR GO; GO:0019301; P:rhamnose catabolic process; IEA:InterPro.
DR CDD; cd07771; FGGY_RhuK; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000577; Carb_kinase_FGGY.
DR InterPro; IPR018485; FGGY_C.
DR InterPro; IPR018484; FGGY_N.
DR InterPro; IPR013449; Rhamnulokinase.
DR PANTHER; PTHR10196:SF93; L-RHAMNULOKINASE; 1.
DR PANTHER; PTHR10196; 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.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Kinase {ECO:0000313|EMBL:ACO48099.1};
KW Plasmid {ECO:0000313|EMBL:ACO48099.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002208};
KW Rhamnose metabolism {ECO:0000256|ARBA:ARBA00023308};
KW Transferase {ECO:0000313|EMBL:ACO48099.1}.
FT DOMAIN 14..251
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 262..450
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 497 AA; 53364 MW; 1903235F614D80DA CRC64;
MSAEATLTDV KRHVAIDLGA SSGRVALGTV HAGKLTVEVL HRFPNGGIPV QGGLYWDVLG
LWREILHGLR LAAGHGPIDS VGVDSWAVDY ALIDEHGLLI DGVRHYRDAR TDGVMDQLLG
VLPRDAVYEF TGIQFLPFNT AFQLVAHRQQ APTQLDRART LLMVPDLLHY WLTGRQVTEM
TNASTTQLYD SRQTAWSEPV LNAFGIPAHL LPDVVHPGTD LGAVQPDVAR DTGLHGTRVI
APGTHDTASA VAAVPADGKG WAYLSSGTWS LVGVETDRPV ITPQALALNL TNEAGVHGTT
RLLKNVMGLW IAQECSRAWG NPSFAELYGA AALVEANGPL IDPDDVRFLP PGLDMPARVQ
AYCAETGQVV PSTPAEITRC VLESLAFRCA EVLSQLEEVT GESIHTLHVV GGGSQIRFLN
QLLADISGRT VVAGPVEATL LGNLLVQAEA CGSIPRGSMR EVSRICEILT TYTPVKKRTV
TQHTIFAELT TRHAAST
//
