ID A0A0Q5ND70_9MICO Unreviewed; 605 AA.
AC A0A0Q5ND70;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=ASF89_01940 {ECO:0000313|EMBL:KQR66714.1};
OS Frigoribacterium sp. Leaf172.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frigoribacterium.
OX NCBI_TaxID=1736285 {ECO:0000313|EMBL:KQR66714.1, ECO:0000313|Proteomes:UP000051720};
RN [1] {ECO:0000313|EMBL:KQR66714.1, ECO:0000313|Proteomes:UP000051720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf172 {ECO:0000313|EMBL:KQR66714.1,
RC ECO:0000313|Proteomes:UP000051720};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR66714.1, ECO:0000313|Proteomes:UP000051720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf172 {ECO:0000313|EMBL:KQR66714.1,
RC ECO:0000313|Proteomes:UP000051720};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQR66714.1}.
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DR EMBL; LMPB01000001; KQR66714.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q5ND70; -.
DR STRING; 1736285.ASF89_01940; -.
DR OrthoDB; 9805576at2; -.
DR UniPathway; UPA00145; UER00566.
DR Proteomes; UP000051720; 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; 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 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:UP000051720};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00520,
KW ECO:0000256|RuleBase:RU003455}.
FT DOMAIN 34..305
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 318..515
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 605 AA; 63281 MW; B56750FE52962853 CRC64;
MVDHVPPATP DETGDGPVAG GSGPTAPGAS TETYVVGVDY GTLSGRAVVV RVSDGAELGA
GVFEYPHAVV DTTLPGTGER LPADWALQVP SDYVDVLKNA VPEALAASGV DPAAVVGIGT
DFTACTMVPT TADGTPLNEL DRFASHPHAF VKLWRHHAAQ GQADRINELA AERGESWLPR
YGGLISSEWE FAKGLQLLEE DPEVYAATEH WVEAADWIVW QLSGRYVRNA CTAGYKGIYQ
DGEYPSREFL AALNPDFADF AETKVVHEIG ALGDSAGTLT AEAAGWTGLP EGIAVAVGNV
DAHVTAPAAK ATQPGQMVAI MGTSTCHVMN GDKLAEVPGM CGVVDGGIVD GLYGYEAGQS
GVGDIFAWYV KNQVPQSAVD DAAAAGKSVH QHLTDVAYEQ PVGAHGLVAL DWHSGNRSVL
VDHELSGVIV GQTLATSPAD GYRALLEATA FGTRRIVQAF DESGVPVTEF IAAGGLLKNK
HLMQTYSDVL RMPISTITSE QGPALGSAIH AAVAAGAYAD IRAAAEAMGS VERATYTPDP
ANADAYDALY AEYLLLHDWF GRGGNDVMHR LRAMRREATR ASSTPGSDSD SDSVEQAAVD
AEVSA
//
