ID   ARAB_BACSU              Reviewed;         560 AA.
AC   P94524; O05185;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   04-NOV-2026, entry version 150.
DE   RecName: Full=Ribulokinase;
DE            EC=2.7.1.16;
GN   Name=araB; OrderedLocusNames=BSU28790;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9084180; DOI=10.1099/00221287-143-3-957;
RA   Sa-Nogueira I.M.G., Nogueira T.V., Soares S., de Lencastre H.;
RT   "The Bacillus subtilis L-arabinose (ara) operon: nucleotide sequence,
RT   genetic organization and expression.";
RL   Microbiology 143:957-969(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA   Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA   Emmerson P.T., Harwood C.R.;
RT   "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT   chromosome containing genes responsible for stress responses, the
RT   utilization of plant cell walls and primary metabolism.";
RL   Microbiology 142:3067-3078(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   TRANSCRIPTIONAL REGULATION.
RX   PubMed=10417639; DOI=10.1046/j.1365-2958.1999.01484.x;
RA   Mota L.J., Tavares P., Sa-Nogueira I.M.G.;
RT   "Mode of action of AraR, the key regulator of L-arabinose metabolism in
RT   Bacillus subtilis.";
RL   Mol. Microbiol. 33:476-489(1999).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-ribulose + ATP = D-ribulose 5-phosphate + ADP + 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;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-ribulose + ATP = L-ribulose 5-phosphate + ADP + H(+);
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;
CC   -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC       ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route):
CC       step 2/3.
CC   -!- INDUCTION: Transcription is repressed by glucose and by the binding of
CC       AraR to the operon promoter. L-arabinose acts as an inducer by
CC       inhibiting the binding of AraR to the DNA, thus allowing expression of
CC       the gene. {ECO:0000269|PubMed:10417639}.
CC   -!- SIMILARITY: Belongs to the ribulokinase family. {ECO:0000305}.
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DR   EMBL; X89408; CAA61586.1; -; Genomic_DNA.
DR   EMBL; Z75208; CAA99588.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14839.1; -; Genomic_DNA.
DR   PIR; D69587; D69587.
DR   RefSeq; NP_390757.1; NC_000964.3.
DR   RefSeq; WP_003229500.1; NC_000964.3.
DR   AlphaFoldDB; P94524; -.
DR   SMR; P94524; -.
DR   FunCoup; P94524; 422.
DR   STRING; 224308.BSU28790; -.
DR   PaxDb; 224308-BSU28790; -.
DR   DNASU; 936019; -.
DR   EnsemblBacteria; CAB14839; CAB14839; BSU_28790.
DR   GeneID; 936019; -.
DR   KEGG; bsu:BSU28790; -.
DR   PATRIC; fig|224308.179.peg.3127; -.
DR   eggNOG; COG1069; Bacteria.
DR   InParanoid; P94524; -.
DR   OMA; AAACNWI; -.
DR   OrthoDB; 9805576at2; -.
DR   PhylomeDB; P94524; -.
DR   BioCyc; BSUB:BSU28790-MONOMER; -.
DR   UniPathway; UPA00145; UER00566.
DR   Proteomes; UP000001570; Chromosome.
DR   AbasyAtlas; P94524; -.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0019150; F:D-ribulokinase activity; IBA:GO_Central.
DR   GO; GO:0008741; F:ribulokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019321; P:pentose metabolic process; IBA:GO_Central.
DR   CDD; cd07781; ASKHA_NBD_FGGY_L-RBK; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   HAMAP; MF_00520; Ribulokinase; 1.
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   InterPro; IPR005929; Ribulokinase.
DR   NCBIfam; TIGR01234; L-ribulokinase; 1.
DR   NCBIfam; NF003154; PRK04123.1; 1.
DR   PANTHER; PTHR43435:SF4; FGGY CARBOHYDRATE KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43435; RIBULOKINASE; 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   2: Evidence at transcript level;
KW   Arabinose catabolism; ATP-binding; Carbohydrate metabolism; Kinase;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..560
FT                   /note="Ribulokinase"
FT                   /id="PRO_0000198357"
FT   CONFLICT        59
FT                   /note="P -> F (in Ref. 1; CAA61586)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   560 AA;  61010 MW;  DE72A1AB73AF0AEF CRC64;
     MAYTIGVDFG TLSGRAVLVH VQTGEELAAA VKEYRHAVID TVLPKTGQKL PRDWALQHPA
     DYLEVLETTI PSLLEQTGVD PKDIIGIGID FTACTILPID SSGQPLCMLP EYEEEPHSYV
     KLWKHHAAQK HADRLNQIAE EEGEAFLQRY GGKISSEWMI PKVMQIAEEA PHIYEAADRI
     IEAADWIVYQ LCGSLKRSNC TAGYKAMWSE KAGYPSDDFF EKLNPSMKTI TKDKLSGSIH
     SVGEKAGSLT EKMAKLTGLL PGTAVAVANV DAHVSVPAVG ITEPGKMLMI MGTSTCHVLL
     GEEVHIVPGM CGVVDNGILP GYAGYEAGQS CVGDHFDWFV KTCVPPAYQE EAKEKNIGVH
     ELLSEKANHQ APGESGLLAL DWWNGNRSTL VDADLTGMLL GMTLLTKPEE IYRALVEATA
     YGTRMIIETF KESGVPIEEL FAAGGIAEKN PFVMQIYADV TNMDIKISGS PQAPALGSAI
     FGALAAGKEK GGYDDIKKAA ANMGKLKDIT YTPNAENAAV YEKLYAEYKE LVHYFGKENH
     VMKRLKTIKN LQFSSAAKKN
//