ID W7Y9J6_9BACT Unreviewed; 555 AA.
AC W7Y9J6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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 ORFNames=JCM21142_93730 {ECO:0000313|EMBL:GAF05007.1};
OS Saccharicrinis fermentans DSM 9555 = JCM 21142.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC Saccharicrinis.
OX NCBI_TaxID=869213 {ECO:0000313|EMBL:GAF05007.1, ECO:0000313|Proteomes:UP000019402};
RN [1] {ECO:0000313|EMBL:GAF05007.1, ECO:0000313|Proteomes:UP000019402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 21142 {ECO:0000313|EMBL:GAF05007.1,
RC ECO:0000313|Proteomes:UP000019402};
RA Starns D., Oshima K., Suda W., Iino T., Yuki M., Inoue J., Kitamura K.,
RA Iida T., Darby A., Hattori M., Ohkuma M.;
RT "Draft Genome Sequence of Cytophaga fermentans JCM 21142T, a Facultative
RT Anaerobe Isolated from Marine Mud.";
RL Genome Announc. 2:e00206-14(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAF05007.1}.
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DR EMBL; BAMD01000064; GAF05007.1; -; Genomic_DNA.
DR RefSeq; WP_027470817.1; NZ_KI912107.1.
DR AlphaFoldDB; W7Y9J6; -.
DR STRING; 869213.GCA_000517085_00855; -.
DR eggNOG; COG1069; Bacteria.
DR OrthoDB; 9805576at2; -.
DR UniPathway; UPA00145; UER00566.
DR Proteomes; UP000019402; Unassembled WGS sequence.
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; 1.20.58.2240; -; 1.
DR Gene3D; 3.30.420.40; -; 1.
DR HAMAP; MF_00520; Ribulokinase; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000577; Carb_kinase_FGGY.
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.
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:UP000019402};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00520,
KW ECO:0000256|RuleBase:RU003455}.
FT DOMAIN 293..504
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 555 AA; 60519 MW; E76579CA0BAB9F0F CRC64;
MKKQYVIGLD YGSDSARSVV VDVANGNELA SSVKYYPRWM EGKYCAPEKD LYRQHPLDYV
EVMEYVVNDA LKKAGEGVAD NVIGISFDTT GSTPVLVNKE GTPLALLPEF AENPNAMFVL
WKDHTAVKEA AEINQLAARW SEDYTKFEGG IYSSEWVWAK ILHVLRSDET VRKASFSWVE
HCDWLPGLIT GNQNPLEILR SRCAAGHKAM WHPGWGGLPS QEFLSELDPV LDGYRERLYK
DTYPSDVAVG NLSKEWAKRL GLTTNVKVGV GAFDCHMGAV GGEVTPNVLV RAIGTSTCDI
MIEEYDKIGD KLIAGICGQV DGSVVPGYVG LEAGQSAFGD LYAWFKHVLA WPIENILAKT
TLVNDKIKTK LMQETMDAII VELSNEAMKI PVEESTIVAV DWMNGRRTPD ASQEVTGSIA
GLKLGSSAPG IFRALVEATA FGSKAIVNRF ASEGVEIKEI IALGGVAKKS PFVMQILADV
LGMSLKVAAT DQTCAFGAAM FAAVVGGAYD RVEDAQKAMG KGFEKVYQPN AKNVEVYGTI
YDKYLKLGAF TESEL
//
