ID   ARAB_PECCP              Reviewed;         566 AA.
AC   C6DH20;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 65.
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=PC1_2028;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001657; ACT13069.1; -; Genomic_DNA.
DR   RefSeq; WP_015840262.1; NC_012917.1.
DR   AlphaFoldDB; C6DH20; -.
DR   SMR; C6DH20; -.
DR   STRING; 561230.PC1_2028; -.
DR   EnsemblBacteria; ACT13069; ACT13069; PC1_2028.
DR   KEGG; pct:PC1_2028; -.
DR   eggNOG; COG1069; Bacteria.
DR   HOGENOM; CLU_009281_9_1_6; -.
DR   OMA; GHKAMWH; -.
DR   OrthoDB; 1619686at2; -.
DR   UniPathway; UPA00145; UER00566.
DR   Proteomes; UP000002736; 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; Transferase.
FT   CHAIN           1..566
FT                   /note="Ribulokinase"
FT                   /id="PRO_1000211745"
SQ   SEQUENCE   566 AA;  61892 MW;  7D060918245E3483 CRC64;
     MSAGAITIGL DFGSDSVRAL AVDCQSGQEL ETEVVYYPRW REGKYCQPAN NQFRHHPLDY
     IESLEQAIKV VVSRLTNEQR QHIIGIGVDS TGSTPAPIDE HGQILALRPE FADNPNAMFV
     LWKDHTAIEE AEAINTLCRS GQFPDYTRYI GGVYSSEWFW AKILHVSRED AAVRQAAVSW
     IELCDWVPAL LSGTQAPADI RRGRCSAGHK SLWHPSWGGL PPKDFLHALD PCLTETLQYP
     LFTDTWTAEQ PVGTITAEWA QRLGIPETVI LAGGAFDCHV GTVGAGAQPY TLVKVIGTST
     CDILIADDAR IADRTIAGIC GQVDGSVIPG YIGLEAGQSA FGDMYAWFGR LLGWSLQEAA
     KDYAEQGHPE LKTSLQAMEA KLLERLTRCW AENPTLDHLP VVLDWFNGRR TPFANQRLKG
     VITDLNLGTD APTLFGGFIA ATAFGARAIM ECFEDQGVPV ENVLALGGIA RKSPVIMQVC
     TDVMNRPLQI VASDQCCALG AAIFAAVAAG VHCDIPTAQQ HMASGIERTL MPDSQRVARY
     QQLYARYQQW CRLAEPAYSP TSTAKN