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Database: UniProt
Entry: S9R7B3_9RHOB
LinkDB: S9R7B3_9RHOB
Original site: S9R7B3_9RHOB 
ID   S9R7B3_9RHOB            Unreviewed;       501 AA.
AC   S9R7B3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Sugar (Pentulose and hexulose) kinase {ECO:0000313|EMBL:EPX87787.1};
DE            EC=2.7.1.53 {ECO:0000313|EMBL:EPX87787.1};
GN   ORFNames=ruthe_00190 {ECO:0000313|EMBL:EPX87787.1};
OS   Rubellimicrobium thermophilum DSM 16684.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Rubellimicrobium.
OX   NCBI_TaxID=1123069 {ECO:0000313|EMBL:EPX87787.1, ECO:0000313|Proteomes:UP000015346};
RN   [1] {ECO:0000313|EMBL:EPX87787.1, ECO:0000313|Proteomes:UP000015346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16684 {ECO:0000313|EMBL:EPX87787.1,
RC   ECO:0000313|Proteomes:UP000015346};
RX   PubMed=24501632; DOI=10.4056/sigs.4247911;
RA   Fiebig A., Riedel T., Gronow S., Petersen J., Klenk H.P., Goker M.;
RT   "Genome sequence of the reddish-pigmented Rubellimicrobium thermophilum
RT   type strain (DSM 16684(T)), a member of the Roseobacter clade.";
RL   Stand. Genomic Sci. 8:480-490(2013).
CC   -!- SIMILARITY: Belongs to the FGGY kinase family.
CC       {ECO:0000256|RuleBase:RU003733}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPX87787.1}.
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DR   EMBL; AOLV01000002; EPX87787.1; -; Genomic_DNA.
DR   RefSeq; WP_021096332.1; NZ_KE557318.1.
DR   AlphaFoldDB; S9R7B3; -.
DR   STRING; 1123069.ruthe_00190; -.
DR   PATRIC; fig|1123069.3.peg.197; -.
DR   HOGENOM; CLU_009281_3_1_5; -.
DR   OrthoDB; 9805576at2; -.
DR   Proteomes; UP000015346; Unassembled WGS sequence.
DR   GO; GO:0008744; F:L-xylulokinase activity; IEA:UniProtKB-EC.
DR   CDD; cd07802; FGGY_L-XK; 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:SF3; L-XYLULOSE/3-KETO-L-GULONATE KINASE; 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:EPX87787.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015346};
KW   Transferase {ECO:0000256|RuleBase:RU003733, ECO:0000313|EMBL:EPX87787.1}.
FT   DOMAIN          6..248
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          258..446
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
SQ   SEQUENCE   501 AA;  52471 MW;  EE511D225000ECEB CRC64;
     MVDTCLLGID SGLTMTKAVV FDAGGRVLAT ARRRIAQSVP RARHVERDMA ALWQATAKAV
     RAALDAAGQP GIAAVAATAH GDGLYLLDRT AQPLCPGILS LDSRAVDAVA RWQADGTADA
     ALSLTGQRPH ASAPSALLAW IRDHEPDRFA RIGHVLACKD WLRFCLTGTI GTDLTEASTA
     FTEVTSQSYA PAILELYGLG ALAPALPPVA RPDQVVGAVT EQAAAMTGLV AGTPVVAGLH
     DVTASALGIG GHRLGCVAIV AGTYSINETV SDRPRTDPRW FCRNGLRPGE WNNMAISPAS
     AANYDWFLDT LTGADRATAE AGGRSIHAAV EPEVRAALNR PSTVLFHPYL YGSPHGPQAS
     GGFLGLHGWH DRGDLIRAVI EGIAFNHRVH IDALREGFAP SQARLTGGIS RSPLYAQVFA
     DALGLPVTVT DTDEAAAWGA ALCAGAGVGL FADPTADPRE LGLVTYAPDP ARSAALQDRY
     RLHCDLAAAL APFWPRIEAP A
//
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