ARAB_SHIDS
ID ARAB_SHIDS Reviewed; 566 AA.
AC Q32K30;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Ribulokinase {ECO:0000255|HAMAP-Rule:MF_00520};
DE EC=2.7.1.16 {ECO:0000255|HAMAP-Rule:MF_00520};
GN Name=araB {ECO:0000255|HAMAP-Rule:MF_00520}; OrderedLocusNames=SDY_0090;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribulose = ADP + D-ribulose 5-phosphate + H(+);
CC Xref=Rhea:RHEA:17601, ChEBI:CHEBI:15378, ChEBI:CHEBI:17173,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58121, ChEBI:CHEBI:456216;
CC EC=2.7.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00520};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-ribulose = ADP + H(+) + L-ribulose 5-phosphate;
CC Xref=Rhea:RHEA:22072, ChEBI:CHEBI:15378, ChEBI:CHEBI:16880,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58226, ChEBI:CHEBI:456216;
CC EC=2.7.1.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00520};
CC -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route):
CC step 2/3. {ECO:0000255|HAMAP-Rule:MF_00520}.
CC -!- SIMILARITY: Belongs to the ribulokinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00520}.
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DR EMBL; CP000034; ABB60327.1; -; Genomic_DNA.
DR RefSeq; WP_000951876.1; NC_007606.1.
DR RefSeq; YP_401816.1; NC_007606.1.
DR AlphaFoldDB; Q32K30; -.
DR SMR; Q32K30; -.
DR STRING; 300267.SDY_0090; -.
DR EnsemblBacteria; ABB60327; ABB60327; SDY_0090.
DR KEGG; sdy:SDY_0090; -.
DR PATRIC; fig|300267.13.peg.105; -.
DR HOGENOM; CLU_009281_9_1_6; -.
DR OMA; GHKAMWH; -.
DR UniPathway; UPA00145; UER00566.
DR Proteomes; UP000002716; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019150; F:D-ribulokinase activity; IEA:RHEA.
DR GO; GO:0008741; F:ribulokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; IEA:UniProtKB-UniRule.
DR CDD; cd07781; FGGY_RBK; 1.
DR HAMAP; MF_00520; Ribulokinase; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018485; Carb_kinase_FGGY_C.
DR InterPro; IPR005929; Ribulokinase.
DR Pfam; PF02782; FGGY_C; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR01234; L-ribulokinase; 1.
PE 3: Inferred from homology;
KW Arabinose catabolism; ATP-binding; Carbohydrate metabolism; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..566
FT /note="Ribulokinase"
FT /id="PRO_0000263405"
SQ SEQUENCE 566 AA; 61381 MW; B78B27DA3E63E926 CRC64;
MAIAIGLDFG SDSVRALAVD CTTGEEIATS VEWYPRWQKG QFCDAPNNQF RHHPRDYIES
MEAALKTVLA ELSVEQRAAV VRIGVDSTGS TPAPIDADGN VLALRPEFAE NPNAMFVLWK
DHTAVEEAEE ITRLCHALGN VDYSRYIGGI YSSEWFWAKI LHVTRQDSAV AQSAASWIEL
CDWVPALLSG TTRPQDIRRG RCSAGHKSLW HESWGGLPPA SFFDELDPIL NRHLPSPLFT
DTWTADIPVG TLCPEWAQRL GLPESVVISG GAFDCHMGAV GAGAQPNALV KVISTSTCDI
LIADKQSVGE RAVKGICGQV DGSVVPGFIG LEAGQSAFGD IYAWFGRVLG WPLEQLAAHH
PELKEQINAS QKQLLPALTE AWAKNPSLDH LPVVLDWFNG RRTPNANQRL KGVITDLNLA
TDAPLLFGGL IAATAFGARA IMECFTDQGI AVNNVMALGG IARKNQVIMQ ACCDVLNRPL
QIVASDQCCA LGAAIFAAVA AKVHADIPSA QQKMASAVEK TLQPRSEQAQ RFEQLYRRYQ
QWAMSAEQHY LPTSAPAQAA QAVPTL