ID A0A0J1FH69_9FIRM Unreviewed; 554 AA.
AC A0A0J1FH69;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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_2 {ECO:0000313|EMBL:KLU62750.1};
GN Synonyms=araB {ECO:0000256|HAMAP-Rule:MF_00520};
GN ORFNames=CEB3_c08400 {ECO:0000313|EMBL:KLU62750.1};
OS Peptococcaceae bacterium CEB3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=999898 {ECO:0000313|EMBL:KLU62750.1, ECO:0000313|Proteomes:UP000035957};
RN [1] {ECO:0000313|EMBL:KLU62750.1, ECO:0000313|Proteomes:UP000035957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEB3 {ECO:0000313|EMBL:KLU62750.1,
RC ECO:0000313|Proteomes:UP000035957};
RA Poehlein A., Petzsch P., Johnson B.D., Schloemann M., Daniel R.,
RA Muehling M.;
RT "Genome sequence of the moderately acidophilic sulfate reducing
RT Peptococcaceae bacterium strain CEB3.";
RL Submitted (JUN-2015) 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}.
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:KLU62750.1}.
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DR EMBL; LDXJ01000038; KLU62750.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J1FH69; -.
DR STRING; 999898.CEB3_c08400; -.
DR PATRIC; fig|999898.3.peg.974; -.
DR OrthoDB; 9805576at2; -.
DR UniPathway; UPA00145; UER00566.
DR Proteomes; UP000035957; 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; 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 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}; 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:UP000035957};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00520,
KW ECO:0000256|RuleBase:RU003455}.
FT DOMAIN 3..274
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 286..485
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 554 AA; 60911 MW; 307624340585B378 CRC64;
MAYAIGVDYG TQSGRVILLD LHSGHEKAIS VVPYKHGVID SVLPTTGTKL PVDWALQDPS
DYLEVLHEGI PMVMREGKVN AGDVIGLGVD FTSCTVLPVN EDGMPLCLMS RWQNHPHAWP
KLWKHHSAQP IADRINQVAE RRGEEFLSRY GGRISAEWYF PKLIEVFEED REVYNACYRF
VEATDWIVWY LTGEERRNSC TAGYKAMWSE HEGIPGTEFF ASVSSEFVNP KEKLGEVFYP
LGTRAGYLKG AVADKLQLHS GVAVAVGNVD AMVSVPSVGV KGLGALVMVM GTSICHLAVT
KEESRFEGIT GVVKDGVLPG YYGYEAGQAA VGDMFEWFVK KLVPQAYFKA AASYKVSIFE
HLENLAAKLL PGESGLIALD WWNGNRSILG DADLSGIILG FTLSTAPEAI YRTLLESTAF
GTRRIVENFT EHGVAIDRLV ACGGLAQRSP LLMRIYADAC GLPVSVASST EIPARGSAMF
GAVAAGKEHG GFESITEASQ HLVSPVLKSY LPEEVVHRKY NELYQIYREI HDFFGIERVD
ILHRLKGIRM NSAV
//
