ID   A1RAY3_PAEAT            Unreviewed;       578 AA.
AC   A1RAY3;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   02-SEP-2026, entry version 131.
DE   RecName: Full=Ribulokinase {ECO:0000256|HAMAP-Rule:MF_00520, ECO:0000256|NCBIfam:TIGR01234};
DE            EC=2.7.1.16 {ECO:0000256|HAMAP-Rule:MF_00520, ECO:0000256|NCBIfam:TIGR01234};
GN   Name=araB {ECO:0000256|HAMAP-Rule:MF_00520,
GN   ECO:0000313|EMBL:ABM08456.1};
GN   OrderedLocusNames=AAur_3709 {ECO:0000313|EMBL:ABM08456.1};
OS   Paenarthrobacter aurescens (strain TC1).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Micrococcaceae; Paenarthrobacter.
OX   NCBI_TaxID=290340 {ECO:0000313|EMBL:ABM08456.1, ECO:0000313|Proteomes:UP000000637};
RN   [1] {ECO:0000313|EMBL:ABM08456.1, ECO:0000313|Proteomes:UP000000637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC1 {ECO:0000313|EMBL:ABM08456.1,
RC   ECO:0000313|Proteomes:UP000000637};
RX   PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA   Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA   Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V., Khouri H.,
RA   Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT   "Secrets of soil survival revealed by the genome sequence of Arthrobacter
RT   aurescens TC1.";
RL   PLoS Genet. 2:2094-2106(2006).
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; Evidence={ECO:0000256|HAMAP-Rule:MF_00520};
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; Evidence={ECO:0000256|HAMAP-Rule:MF_00520,
CC         ECO:0000256|RuleBase:RU003455};
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:0000256|HAMAP-Rule:MF_00520,
CC       ECO:0000256|RuleBase:RU003455}.
CC   -!- SIMILARITY: Belongs to the ribulokinase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00520, ECO:0000256|RuleBase:RU003455}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000474; ABM08456.1; -; Genomic_DNA.
DR   RefSeq; WP_011776321.1; NC_008711.1.
DR   AlphaFoldDB; A1RAY3; -.
DR   STRING; 290340.AAur_3709; -.
DR   KEGG; aau:AAur_3709; -.
DR   eggNOG; COG1069; Bacteria.
DR   HOGENOM; CLU_009281_9_1_11; -.
DR   OrthoDB; 9805576at2; -.
DR   UniPathway; UPA00145; UER00566.
DR   Proteomes; UP000000637; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019150; F:D-ribulokinase activity; IEA:TreeGrafter.
DR   GO; GO:0008741; F:ribulokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046835; P:carbohydrate phosphorylation; IEA:TreeGrafter.
DR   GO; GO:0019569; P:L-arabinose catabolic process to D-xylulose 5-phosphate; IEA:UniProtKB-UniRule.
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; 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   3: Inferred from homology;
KW   Arabinose catabolism {ECO:0000256|ARBA:ARBA00022935, ECO:0000256|HAMAP-
KW   Rule:MF_00520};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00520};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW   Rule:MF_00520};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00520};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00520}; Reference proteome {ECO:0000313|Proteomes:UP000000637};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00520}.
FT   DOMAIN          14..284
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          297..494
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
SQ   SEQUENCE   578 AA;  61699 MW;  C57C552761FB3BB0 CRC64;
     MNTSENIPLD EQFVIGVDYG TLSGRAVVVR VSDGAEIGSG VFEYPHAVVT DNLPGSSQRL
     PADWALQVPN DYRDVLRNAV PAAVADAGIN PENVVGIGTD FTACTMVPTT ADGTPLNELE
     RFADRPHAFV KLWRHHAAQP QADRINQLAA ERGESWLPRY GGLISSEWEF AKGLQLLEED
     PEVYGAMEHW VEAADWIVWQ LCGSYVRNAC TAGYKGIYQD GKYPSQDFLT ALNPDFKDFV
     SEKLEHTIGR LGDAAGYLTE EAAAWTGLPA GIAVAVGNVD AHVSAPAANA VEPGQLVAIM
     GTSTCHVMNG DVLREVPGMC GVVDGGIVDG LWGYEAGQSG VGDIFGWFTK NGVPPEYHQA
     AKDKGLGIHE YLTELAEKQA IGEHGLIALD WHSGNRSVLV DHELSGVVVG QTLATKPEDT
     YRALLEATAF GTRTIVDAFR DSGVPVKEFI VAGGLLKNKF LMQVYADITG LQLSTIGSEQ
     GPALGSAIHA AVAAGKYKDI REAASSMAAA PGAVYTPIPE NVAAYEVLFQ EYRTLHDYFG
     RGTNNVMHRL KAIQRAAIQG SSHNGPAAQA STLEGASA
//