ID K9ZXF3_DEIPD Unreviewed; 548 AA.
AC K9ZXF3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=Ribulokinase {ECO:0000256|HAMAP-Rule:MF_00520, ECO:0000256|RuleBase:RU003455};
DE EC=2.7.1.16 {ECO:0000256|HAMAP-Rule:MF_00520, ECO:0000256|RuleBase:RU003455};
GN Name=araB {ECO:0000256|HAMAP-Rule:MF_00520};
GN OrderedLocusNames=Deipe_0761 {ECO:0000313|EMBL:AFZ66338.1};
OS Deinococcus peraridilitoris (strain DSM 19664 / LMG 22246 / CIP 109416 /
OS KR-200).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=937777 {ECO:0000313|EMBL:AFZ66338.1, ECO:0000313|Proteomes:UP000010467};
RN [1] {ECO:0000313|Proteomes:UP000010467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19664 / LMG 22246 / CIP 109416 / KR-200
RC {ECO:0000313|Proteomes:UP000010467};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Lu M.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Pukall R., Steenblock K., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Deinococcus peraridilitoris DSM
RT 19664.";
RL Submitted (MAR-2012) 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:0000256|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: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}.
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DR EMBL; CP003382; AFZ66338.1; -; Genomic_DNA.
DR RefSeq; WP_015234648.1; NC_019793.1.
DR AlphaFoldDB; K9ZXF3; -.
DR STRING; 937777.Deipe_0761; -.
DR KEGG; dpd:Deipe_0761; -.
DR PATRIC; fig|937777.3.peg.767; -.
DR eggNOG; COG1069; Bacteria.
DR HOGENOM; CLU_009281_9_1_0; -.
DR OMA; GHKAMWH; -.
DR OrthoDB; 9805576at2; -.
DR UniPathway; UPA00145; UER00566.
DR Proteomes; UP000010467; 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 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; IPR005929; Ribulokinase.
DR NCBIfam; TIGR01234; L-ribulokinase; 1.
DR PANTHER; PTHR43435:SF4; FGGY CARBOHYDRATE KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43435; RIBULOKINASE; 1.
DR Pfam; PF02782; FGGY_C; 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 Arabinose catabolism {ECO:0000256|ARBA:ARBA00022935, ECO:0000256|HAMAP-
KW Rule:MF_00520}; ATP-binding {ECO:0000256|HAMAP-Rule:MF_00520};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_00520};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00520, ECO:0000256|RuleBase:RU003455};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00520};
KW Reference proteome {ECO:0000313|Proteomes:UP000010467};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00520}.
FT DOMAIN 288..485
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 548 AA; 58651 MW; 231F80DC719C8FC8 CRC64;
MAEQYAVGVD FGSESGRAVV VRLSDGAALG EAVTPYVHAV MDRALPCGTP LGKEWALQHP
QDYLDVFQQA VPAALASSGV HSDDVIGIGI DFTACTPMPT LADGTPLCLL SEHASNPHAW
IKLWKHHAAQ PQADRINAVA LARGEPWLAR YGGKQSSEWF FAKALQILEE DPKLYAATER
FIEAADWVVW QLTGVETRSA CTAGYKAIHQ DGRFPDASFF AALHPDFADV VQTRMKTDLA
PLGGKAGELS EQAAAWTGLN PGTAVAVANV DAHVTLPAAG VTQPGRLVAI MGTSTCHVLL
GDELREVPGM CGVVPDGVVP GLYGYEAGQS GVGDIFAWFV KHGVPPEYHR QAEREGVSVH
DVLEREAALQ APGEHGLVAL DWLNGNRSVL VDANLSGVIL GLSIGTRAPD IYRALIEATA
YGTRLIIETF EASGVPVNEV VIAGGLKKNR LLMQVYADVT GRSLSILDVE QGPALGSAMH
AAVAAGAYPD IFAAAERMGQ VRRDAYRPDP AARATYDKLY AEYRTLHDYF GRGANDVMHR
LKALRRPE
//