RBSKI_FRUSL
ID RBSKI_FRUSL Reviewed; 540 AA.
AC P83534; A0A0R2BNR0;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 2.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Bifunctional ribokinase/ribose-5-phosphate isomerase A {ECO:0000305};
DE Includes:
DE RecName: Full=Ribokinase {ECO:0000250|UniProtKB:P0A9J6};
DE EC=2.7.1.15 {ECO:0000250|UniProtKB:P0A9J6};
DE Includes:
DE RecName: Full=Ribose-5-phosphate isomerase A {ECO:0000250|UniProtKB:P0A7Z0};
DE EC=5.3.1.6 {ECO:0000250|UniProtKB:P0A7Z0};
DE AltName: Full=Phosphoriboisomerase A;
DE Short=PRI;
GN Name=rbsK/rbiA; ORFNames=FD36_GL000739;
OS Fructilactobacillus sanfranciscensis (strain ATCC 27651 / DSM 20451 / JCM
OS 5668 / CCUG 30143 / KCTC 3205 / NCIMB 702811 / NRRL B-3934 / L-12)
OS (Lactobacillus sanfranciscensis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Fructilactobacillus.
OX NCBI_TaxID=1423800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27651 / DSM 20451 / JCM 5668 / CCUG 30143 / KCTC 3205 / NCIMB
RC 702811 / NRRL B-3934 / L-12;
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).
RN [2]
RP PROTEIN SEQUENCE OF 245-267, AND INDUCTION.
RC STRAIN=ATCC 27651 / DSM 20451 / JCM 5668 / CCUG 30143 / KCTC 3205 / NCIMB
RC 702811 / NRRL B-3934 / L-12;
RX PubMed=12112860;
RX DOI=10.1002/1615-9861(200206)2:6<765::aid-prot765>3.0.co;2-v;
RA Drews O., Weiss W., Reil G., Parlar H., Wait R., Goerg A.;
RT "High pressure effects step-wise altered protein expression in
RT Lactobacillus sanfranciscensis.";
RL Proteomics 2:765-774(2002).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the phosphorylation of
CC ribose at O-5 in a reaction requiring ATP and magnesium, and the
CC reversible conversion of ribose 5-phosphate to ribulose 5-phosphate.
CC {ECO:0000250|UniProtKB:P0A7Z0}.
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:0000250|UniProtKB:P0A9J6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate;
CC Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273;
CC EC=5.3.1.6; Evidence={ECO:0000250|UniProtKB:P0A7Z0};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0A9J6};
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:0000250|UniProtKB:P0A9J6};
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. Also activated by ammonium ion. Ion binding induces
CC a conformational change that may alter substrate affinity.
CC {ECO:0000250|UniProtKB:P0A9J6}.
CC -!- PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-
CC phosphate from beta-D-ribopyranose: step 2/2.
CC {ECO:0000250|UniProtKB:P0A9J6}.
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribose
CC 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step
CC 1/1. {ECO:0000250|UniProtKB:P0A7Z0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A9J6}.
CC -!- INDUCTION: By elevated hydrostatic pressure.
CC {ECO:0000269|PubMed:12112860}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the carbohydrate
CC kinase PfkB family. Ribokinase subfamily. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the ribose 5-
CC phosphate isomerase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AYYM01000003; KRM80848.1; -; Genomic_DNA.
DR RefSeq; WP_056957679.1; NZ_MIYJ01000023.1.
DR AlphaFoldDB; P83534; -.
DR SMR; P83534; -.
DR GeneID; 57099720; -.
DR PATRIC; fig|1423800.3.peg.750; -.
DR UniPathway; UPA00115; UER00412.
DR UniPathway; UPA00916; UER00889.
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; 3.40.1190.20; -; 1.
DR HAMAP; MF_01987; Ribokinase; 1.
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 Pfam; PF00294; PfkB; 1.
DR Pfam; PF06026; Rib_5-P_isom_A; 1.
DR PRINTS; PR00990; RIBOKINASE.
DR SUPFAM; SSF100950; SSF100950; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR02152; D_ribokin_bact; 1.
DR TIGRFAMs; TIGR00021; rpiA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Carbohydrate metabolism; Cytoplasm; Direct protein sequencing;
KW Isomerase; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Potassium;
KW Transferase.
FT CHAIN 1..540
FT /note="Bifunctional ribokinase/ribose-5-phosphate isomerase
FT A"
FT /id="PRO_0000285983"
FT REGION 1..308
FT /note="Ribokinase"
FT REGION 309..540
FT /note="Ribose-5-phosphate isomerase A"
FT ACT_SITE 253
FT /note="Proton acceptor; for ribokinase activity"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
FT ACT_SITE 417
FT /note="Proton acceptor; for ribose-5-phosphate isomerase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P0A7Z0"
FT BINDING 11..13
FT /ligand="substrate"
FT /ligand_note="for ribokinase activity"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
FT BINDING 39..44
FT /ligand="substrate"
FT /ligand_note="for ribokinase activity"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
FT BINDING 141
FT /ligand="substrate"
FT /ligand_note="for ribokinase activity"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
FT BINDING 185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
FT BINDING 221..226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
FT BINDING 247
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
FT BINDING 249
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
FT BINDING 252..253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
FT BINDING 253
FT /ligand="substrate"
FT /ligand_label="1"
FT /ligand_note="for ribokinase activity"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
FT BINDING 284
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
FT BINDING 287
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
FT BINDING 289
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
FT BINDING 293
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
FT BINDING 339..342
FT /ligand="substrate"
FT /ligand_label="2"
FT /ligand_note="for ribose-5-phosphate isomerase activity"
FT /evidence="ECO:0000250|UniProtKB:P0A7Z0"
FT BINDING 395..398
FT /ligand="substrate"
FT /ligand_label="2"
FT /ligand_note="for ribose-5-phosphate isomerase activity"
FT /evidence="ECO:0000250|UniProtKB:P0A7Z0"
FT BINDING 408..411
FT /ligand="substrate"
FT /ligand_label="2"
FT /ligand_note="for ribose-5-phosphate isomerase activity"
FT /evidence="ECO:0000250|UniProtKB:P0A7Z0"
FT BINDING 435
FT /ligand="substrate"
FT /ligand_label="2"
FT /ligand_note="for ribose-5-phosphate isomerase activity"
FT /evidence="ECO:0000250|UniProtKB:P0A7Z0"
FT CONFLICT 256
FT /note="I -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="Q -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="I -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="L -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 540 AA; 58137 MW; 8FB6CC65FBC243E8 CRC64;
MKKIIVVGST NVDKVLNVEK YALPGETLAI NTYQQSHGGG KGANQAIAAA RSGADTTFIT
KLGNDEDAKM MVKGFKADGM NIDDVITTTD QETGKAYITV DKSGQNSIYV YGGANMAMTP
TDVDAHKSAI INADRVIAQL EIPVPAVIEA FKIAKEHGVQ TILNPAPAKE LPEELLKLTD
IITPNESEAA TLTGIEVKDE TSMLANAKFF FERGIKMVII TVGGRGSFFA TPDDHALIPP
FPAKVVDTTA AGDTFIGSLA SQLEIDLSNI RKAMLYASHA SSLTIQVAGA QNSIPTREAI
LNVINQDQMT KTEIEKQKAQ AAAYAAKLVP DHIVLGLGSG TTAAYFVKAI NQRINDEHLD
IQCVATSVGT EKLAEKLGMR MLDVNTIDQV DLTVDGADVV DHQLNGIKGG GAALLFEKLV
ADMSKQNIWI VDQSKYTDSL AGHILTIEVI PFGGMGVFRY LKENGYQPEF RFKDNGDILE
TDSGNYLINI IIPKDADLEK LSIDLKKQTG VVEHGLFLNV CDELIIGGDQ IKTIKRSDLS
