ARAB_ANOFW
ID ARAB_ANOFW Reviewed; 564 AA.
AC B7GGV9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Ribulokinase {ECO:0000255|HAMAP-Rule:MF_00520};
DE EC=2.7.1.16 {ECO:0000255|HAMAP-Rule:MF_00520};
GN Name=araB {ECO:0000255|HAMAP-Rule:MF_00520}; OrderedLocusNames=Aflv_0530;
OS Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=491915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21510 / WK1;
RX PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT "Encapsulated in silica: genome, proteome and physiology of the
RT thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL Genome Biol. 9:R161.1-R161.16(2008).
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:0000255|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:0000255|HAMAP-Rule:MF_00520};
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:0000255|HAMAP-Rule:MF_00520}.
CC -!- SIMILARITY: Belongs to the ribulokinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00520}.
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DR EMBL; CP000922; ACJ32914.1; -; Genomic_DNA.
DR RefSeq; WP_012574229.1; NC_011567.1.
DR AlphaFoldDB; B7GGV9; -.
DR SMR; B7GGV9; -.
DR STRING; 491915.Aflv_0530; -.
DR EnsemblBacteria; ACJ32914; ACJ32914; Aflv_0530.
DR KEGG; afl:Aflv_0530; -.
DR PATRIC; fig|491915.6.peg.543; -.
DR eggNOG; COG1069; Bacteria.
DR HOGENOM; CLU_009281_9_1_9; -.
DR OMA; GHKAMWH; -.
DR OrthoDB; 1619686at2; -.
DR UniPathway; UPA00145; UER00566.
DR Proteomes; UP000000742; 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 HAMAP; MF_00520; Ribulokinase; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000577; Carb_kinase_FGGY.
DR InterPro; IPR018485; Carb_kinase_FGGY_C.
DR InterPro; IPR018484; Carb_kinase_FGGY_N.
DR InterPro; IPR005929; Ribulokinase.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR PIRSF; PIRSF000538; GlpK; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR01234; L-ribulokinase; 1.
PE 3: Inferred from homology;
KW Arabinose catabolism; ATP-binding; Carbohydrate metabolism; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..564
FT /note="Ribulokinase"
FT /id="PRO_1000127625"
SQ SEQUENCE 564 AA; 61968 MW; 10567BE3E7019125 CRC64;
MGKKYVIGID YGTESGRAVL VDLEGNEIAD HVTPYPHGVI DEVLPESNVQ LEPDWALQHP
GDYIEVLATA VPAVLQKSGV NPADVIGVGI DFTACTMLPI AGSGEPLCLK PEFKHRPHSW
VKLWKHHAAQ DEANLLNEMA AKRGEAFLPR YGGKISSEWM IAKIWQILNE DPDIYDQTDL
FLEATDWVIF KMTGQLVRNS CTAGYKSIWH KQDGYPSKEF FRALDPRLEH VTETKLRGSI
VPLGTRAGVL TKEMAAMMGL LPGTAVAVGN VDAHAAVPGV GVVEPGKMVM AMGTSICHML
LGTEEKYVEG MCGVVEDGII PGYFGYEAGQ SAVGDIFAWY VEQSVPAYVK EAAEKEGVSV
HEWLEKRAAA YRPGETGLLA LDWWNGNRSV LVDTDLTGLI IGYTLLTKPE EIYRALLEAT
AFGTRKIIDA FVESGINVDE LYACGGLPQK NKLLMQIYAD VTNREIKIAA SKQTPAVGAA
MFAAVAAGKE NGGYESIIEA ARNMGKVREE TFKPIPENVA IYEQLYQEYT KLHDYFGRGE
NDVMKRLKHW KETARAVKES ISLS