ID A0A0R2JWH0_9LACO Unreviewed; 543 AA.
AC A0A0R2JWH0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Ribokinase {ECO:0000256|ARBA:ARBA00016943, ECO:0000256|HAMAP-Rule:MF_01987};
DE Short=RK {ECO:0000256|HAMAP-Rule:MF_01987};
DE EC=2.7.1.15 {ECO:0000256|HAMAP-Rule:MF_01987};
GN Name=rbsK {ECO:0000256|HAMAP-Rule:MF_01987};
GN ORFNames=IV52_GL000156 {ECO:0000313|EMBL:KRN80038.1};
OS Fructilactobacillus lindneri DSM 20690 = JCM 11027.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Fructilactobacillus.
OX NCBI_TaxID=1122148 {ECO:0000313|EMBL:KRN80038.1, ECO:0000313|Proteomes:UP000051565};
RN [1] {ECO:0000313|EMBL:KRN80038.1, ECO:0000313|Proteomes:UP000051565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20690 {ECO:0000313|EMBL:KRN80038.1,
RC ECO:0000313|Proteomes:UP000051565};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- FUNCTION: Catalyzes the phosphorylation of ribose at O-5 in a reaction
CC requiring ATP and magnesium. The resulting D-ribose-5-phosphate can
CC then be used either for sythesis of nucleotides, histidine, and
CC tryptophan, or as a component of the pentose phosphate pathway.
CC {ECO:0000256|HAMAP-Rule:MF_01987}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribose = ADP + D-ribose 5-phosphate + H(+);
CC Xref=Rhea:RHEA:13697, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:47013, ChEBI:CHEBI:78346, ChEBI:CHEBI:456216;
CC EC=2.7.1.15; Evidence={ECO:0000256|ARBA:ARBA00000691,
CC ECO:0000256|HAMAP-Rule:MF_01987};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01987};
CC Note=Requires a divalent cation, most likely magnesium in vivo, as an
CC electrophilic catalyst to aid phosphoryl group transfer. It is the
CC chelate of the metal and the nucleotide that is the actual substrate.
CC {ECO:0000256|HAMAP-Rule:MF_01987};
CC -!- ACTIVITY REGULATION: Activated by a monovalent cation that binds near,
CC but not in, the active site. The most likely occupant of the site in
CC vivo is potassium. Ion binding induces a conformational change that may
CC alter substrate affinity. {ECO:0000256|HAMAP-Rule:MF_01987}.
CC -!- PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-
CC phosphate from beta-D-ribopyranose: step 2/2. {ECO:0000256|HAMAP-
CC Rule:MF_01987}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01987}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01987}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family. Ribokinase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01987}.
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:KRN80038.1}.
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DR EMBL; JQBT01000012; KRN80038.1; -; Genomic_DNA.
DR RefSeq; WP_054646641.1; NZ_MIYK01000017.1.
DR AlphaFoldDB; A0A0R2JWH0; -.
DR STRING; 53444.AYR59_00815; -.
DR GeneID; 61249421; -.
DR PATRIC; fig|1122148.6.peg.164; -.
DR OrthoDB; 9775849at2; -.
DR UniPathway; UPA00916; UER00889.
DR Proteomes; UP000051565; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004747; F:ribokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0019303; P:D-ribose catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IEA:InterPro.
DR CDD; cd01174; ribokinase; 1.
DR CDD; cd01398; RPI_A; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR Gene3D; 3.40.50.1360; -; 1.
DR HAMAP; MF_01987; Ribokinase; 1.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR011877; D_ribokin.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR002139; Ribo/fructo_kinase.
DR InterPro; IPR029056; Ribokinase-like.
DR InterPro; IPR004788; Ribose5P_isomerase_type_A.
DR NCBIfam; TIGR02152; D_ribokin_bact; 1.
DR NCBIfam; TIGR00021; rpiA; 1.
DR PANTHER; PTHR10584:SF166; RIBOKINASE; 1.
DR PANTHER; PTHR10584; SUGAR KINASE; 1.
DR Pfam; PF00294; PfkB; 1.
DR Pfam; PF06026; Rib_5-P_isom_A; 1.
DR PRINTS; PR00990; RIBOKINASE.
DR SUPFAM; SSF75445; D-ribose-5-phosphate isomerase (RpiA), lid domain; 1.
DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01987};
KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01987};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01987};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_01987, ECO:0000256|RuleBase:RU003704};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01987};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01987}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01987};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_01987};
KW Reference proteome {ECO:0000313|Proteomes:UP000051565};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01987}.
FT DOMAIN 3..297
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
FT ACT_SITE 254
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 12..14
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 41..45
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 222..227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 248
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 250
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 253..254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 279
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 285
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 288
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 290
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
FT BINDING 294
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01987"
SQ SEQUENCE 543 AA; 58919 MW; 8B527BB6BFBA4734 CRC64;
MTKKIVVVGS TNVDKVLNVD KYALPGETLA INTYQQSHGG GKGANQAIAA ARSGAETTFI
TKLGNDEDAK MMIAGFKQDK MNVDHLITTQ DHETGKAYIT VDKTGQNSIY VYGGANMAMT
PEDVEAHRDA IANADRIIAQ LEIPIPAIIA AFKIAKANGV QTILNPAPAR QLPEELLQLT
DIITPNETES QTLTGIEVKD EVSMLDNAMI FFEKGIKMVI ITVGDKGSFY ATPTEHDFIP
AFKVKAVDTT AAGDTFIGAL ASQLAIDNSN IKEAMLYANH ASSLTVQVAG AQNSIPTEAE
IRNVIKQDSI SKEEIEKEKQ QAAEFAAQQI PNHITLGLGS GTTSAYFVKA IQKRIVNEKL
DIQCVATSLG TQKLAESLHM NMLDVNTIDE VDITVDGADS VDDKLNGIKG GGAALLFEKL
VAKMSKKNIW IVDSTKYHKT LEGRQMPVEV IPFGGMGVFR YLRDNGYHPA FRFEDNGDIL
ETDSGNYLIN ITIPKHADLK DLAKNLKNQT GVVEHGLFLN VCDELIIGGD QIKTIKREDL
ATK
//
