RPIA_STRMU
ID RPIA_STRMU Reviewed; 225 AA.
AC Q8DTT9;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Ribose-5-phosphate isomerase A {ECO:0000255|HAMAP-Rule:MF_00170};
DE EC=5.3.1.6 {ECO:0000255|HAMAP-Rule:MF_00170};
DE AltName: Full=Phosphoriboisomerase A {ECO:0000255|HAMAP-Rule:MF_00170};
DE Short=PRI {ECO:0000255|HAMAP-Rule:MF_00170};
GN Name=rpiA {ECO:0000255|HAMAP-Rule:MF_00170}; OrderedLocusNames=SMU_1234;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS), AND SUBUNIT.
RA Fan X.X., Wang K.T., Su X.D.;
RT "Crystal structure of ribose-5-phosphate isomerase a from str mutans
RT ua159.";
RL Submitted (DEC-2009) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to
CC ribulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00170}.
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:0000255|HAMAP-Rule:MF_00170};
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:0000255|HAMAP-Rule:MF_00170}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00170,
CC ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00170}.
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DR EMBL; AE014133; AAN58919.1; -; Genomic_DNA.
DR RefSeq; NP_721613.1; NC_004350.2.
DR RefSeq; WP_002263209.1; NC_004350.2.
DR PDB; 3L7O; X-ray; 1.70 A; A/B=1-225.
DR PDBsum; 3L7O; -.
DR AlphaFoldDB; Q8DTT9; -.
DR SMR; Q8DTT9; -.
DR STRING; 210007.SMU_1234; -.
DR PRIDE; Q8DTT9; -.
DR EnsemblBacteria; AAN58919; AAN58919; SMU_1234.
DR KEGG; smu:SMU_1234; -.
DR PATRIC; fig|210007.7.peg.1107; -.
DR eggNOG; COG0120; Bacteria.
DR HOGENOM; CLU_056590_1_0_9; -.
DR OMA; YDWDEVN; -.
DR PhylomeDB; Q8DTT9; -.
DR BRENDA; 5.3.1.6; 5941.
DR UniPathway; UPA00115; UER00412.
DR EvolutionaryTrace; Q8DTT9; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IEA:UniProtKB-UniRule.
DR CDD; cd01398; RPI_A; 1.
DR HAMAP; MF_00170; Rib_5P_isom_A; 1.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR InterPro; IPR020672; Ribose5P_isomerase_typA_subgr.
DR InterPro; IPR004788; Ribose5P_isomerase_type_A.
DR Pfam; PF06026; Rib_5-P_isom_A; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR00021; rpiA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Reference proteome.
FT CHAIN 1..225
FT /note="Ribose-5-phosphate isomerase A"
FT /id="PRO_0000158473"
FT ACT_SITE 104
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 26..29
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 82..85
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 95..98
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:3L7O"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:3L7O"
FT HELIX 30..44
FT /evidence="ECO:0007829|PDB:3L7O"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:3L7O"
FT HELIX 55..64
FT /evidence="ECO:0007829|PDB:3L7O"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:3L7O"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:3L7O"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:3L7O"
FT HELIX 101..109
FT /evidence="ECO:0007829|PDB:3L7O"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:3L7O"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:3L7O"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:3L7O"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:3L7O"
FT HELIX 141..150
FT /evidence="ECO:0007829|PDB:3L7O"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:3L7O"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:3L7O"
FT HELIX 184..192
FT /evidence="ECO:0007829|PDB:3L7O"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:3L7O"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:3L7O"
FT TURN 215..218
FT /evidence="ECO:0007829|PDB:3L7O"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:3L7O"
SQ SEQUENCE 225 AA; 24568 MW; 06A854001BCE9D9B CRC64;
MEELKKIAGV RAAQYVEDGM IVGLGTGSTA YYFVEEVGRR VQEEGLQVIG VTTSSRTTAQ
AQALGIPLKS IDEVDSVDVT VDGADEVDPN FNGIKGGGGA LLMEKIVGTL TKDYIWVVDE
SKMVDTLGAF RLPVEVVQYG AERLFREFEK KGYKPSFREY DGVRFVTDMK NFIIDLDLGS
IPDPIAFGNM LDHQVGVVEH GLFNGMVNRV IVAGKDGVRI LEANK
