ARAB_STAES
ID ARAB_STAES Reviewed; 536 AA.
AC Q8CRC6;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 102.
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=SE_1914;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO05555.1; -; Genomic_DNA.
DR RefSeq; NP_765469.1; NC_004461.1.
DR RefSeq; WP_002456635.1; NZ_WBME01000027.1.
DR AlphaFoldDB; Q8CRC6; -.
DR SMR; Q8CRC6; -.
DR STRING; 176280.SE_1914; -.
DR EnsemblBacteria; AAO05555; AAO05555; SE_1914.
DR GeneID; 50017985; -.
DR KEGG; sep:SE_1914; -.
DR PATRIC; fig|176280.10.peg.1872; -.
DR eggNOG; COG1069; Bacteria.
DR HOGENOM; CLU_009281_9_1_9; -.
DR OMA; RPRENHA; -.
DR UniPathway; UPA00145; UER00566.
DR Proteomes; UP000001411; 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.
PE 3: Inferred from homology;
KW Arabinose catabolism; ATP-binding; Carbohydrate metabolism; Kinase;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..536
FT /note="Ribulokinase"
FT /id="PRO_0000198372"
SQ SEQUENCE 536 AA; 60052 MW; 3E5A71EAB682F45B CRC64;
MSYSIGIDFG TASGRVILAD TSNGHIISRY EEDYANGTYM NSLYDKPLPE NYFLQNADDY
LQILEQGVQF VLEDSKVNKN DVVGIGVDFT SSTIIFLDEQ FEPLHRHEDL KTNPHAYVKL
WKHHGAQDEA NYMIQMSKNK NWLDYYGSSV NSEWMIPKIL EVKHEAPEIL RRARYIMEAG
DYITSILTNS NIRSNCGIGF KGFWDNEAGF NYDFFHSVDP DLPKIVKEKC EAPIISIGES
AGRLCKDYQQ IWGLSQDVQV SPFIIDAHSG VLGVGAIEAG EFTAVIGTST CHLMLDSRQV
PISSITGSVK NAIIPGLYAY EAGQPAVGDL FEYSKNQAPK HIVDQANEHH MPVLNYLEEL
ASHIRIEEQH VVVLDWLNGN RSILSNSHLT GSIFGLTLQT PYEMIHRAYI EATAFGTKLI
MKQFEDNHIP VHTVYASGGI PQKSKLLVEI YANVLNKRVV VIDSSNASAL GAAMLGANVG
NAYSTLKEAA LSMKQPIAYI QEPEIQKVQA YKPLYHKYCE LHDLLGRQYP ELSYLI