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Database: UniProt
Entry: E8DWU8_SALMO
LinkDB: E8DWU8_SALMO
Original site: E8DWU8_SALMO 
ID   E8DWU8_SALMO            Unreviewed;       569 AA.
AC   E8DWU8;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 66.
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};
OS   Salmonella enterica subsp. enterica serovar Montevideo str. MB111609-0052.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=871590 {ECO:0000313|EMBL:AEK68952.1};
RN   [1] {ECO:0000313|EMBL:AEK68952.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MB111609-0052 {ECO:0000313|EMBL:AEK68952.1};
RX   PubMed=21345093; DOI=10.1056/NEJMc1100443;
RA   Lienau E.K., Strain E., Wang C., Zheng J., Ottesen A.R., Keys C.E.,
RA   Hammack T.S., Musser S.M., Brown E.W., Allard M.W., Cao G., Meng J.,
RA   Stones R.;
RT   "Identification of a salmonellosis outbreak by means of molecular
RT   sequencing.";
RL   N. Engl. J. Med. 364:981-982(2011).
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}.
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DR   EMBL; JF712376; AEK68952.1; -; Genomic_DNA.
DR   RefSeq; WP_000951817.1; NZ_AETN01000030.1.
DR   AlphaFoldDB; E8DWU8; -.
DR   SMR; E8DWU8; -.
DR   PATRIC; fig|871590.3.peg.3640; -.
DR   UniPathway; UPA00145; UER00566.
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; 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   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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00520}.
FT   DOMAIN          291..501
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
SQ   SEQUENCE   569 AA;  61683 MW;  A62139B451837ACE CRC64;
     MAIAIGLDFG SDSVRALAVD CATGDEIATS VEWYPRWQEG RYCDGPNNQF RHHPRDYMES
     MEAALKAVLA QLSAAQRANV VGIGVDSTGS TPAPIDADGN VLALRPEFAE NPNAMFVLWK
     DHTAVEEADE ITRLCHKPGK VDYSRYIGGI YSSEWFWAKI LHVTRQDSAV AQAAVSWIEL
     CDWVPALLSG TTRPQDIRRG RCSAGHKTLW HESWGGLPPA SFFDELDPCI NRHLRYPLFS
     ETFTADLPVG TLCAEWAQRL GLPESVVISG GAFDCHMGAV GAGAQPNTLV KVIGTSTCDI
     LIADKQSVGD RAVKGICGQV DGSVVPNFIG LEAGQSAFGD IYAWFSRVLS WPLEQLAAQH
     PELKTQINAS QKQLLPALTD AWAKNPSLDH LPVVLDWFNG RRTPNANQRL KGVITDLNLA
     TDAPALFGGL VASTAFGARA IQECFTDQGI AVNNVMALGG IARKNQVIMQ VCCDVLNRPL
     QIVASDQCCA LGAAIFAAVA AKVHADIPAA QQSMASAVER TLRPRPEQAQ RLEQLYRRYQ
     QWALSAEQHY LPTAAPAPTT PANQAILTH
//
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