RPIA_VIBVY
ID RPIA_VIBVY Reviewed; 218 AA.
AC Q7MHL9;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 111.
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=VV2850;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP AND SUBUNIT.
RX PubMed=19214439; DOI=10.1007/s10059-009-0010-6;
RA Kim T.G., Kwon T.H., Min K., Dong M.S., Park Y.I., Ban C.;
RT "Crystal structures of substrate and inhibitor complexes of ribose 5-
RT phosphate isomerase A from Vibrio vulnificus YJ016.";
RL Mol. Cells 27:99-103(2009).
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|PubMed:19214439}.
CC -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00170}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC95614.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BA000037; BAC95614.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_043877321.1; NC_005139.1.
DR PDB; 3ENQ; X-ray; 2.00 A; A/B=1-218.
DR PDB; 3ENV; X-ray; 2.00 A; A/B=1-218.
DR PDB; 3ENW; X-ray; 2.00 A; A/B=1-218.
DR PDBsum; 3ENQ; -.
DR PDBsum; 3ENV; -.
DR PDBsum; 3ENW; -.
DR AlphaFoldDB; Q7MHL9; -.
DR SMR; Q7MHL9; -.
DR STRING; 672.VV93_v1c25580; -.
DR EnsemblBacteria; BAC95614; BAC95614; BAC95614.
DR KEGG; vvy:VV2850; -.
DR eggNOG; COG0120; Bacteria.
DR HOGENOM; CLU_056590_1_1_6; -.
DR OMA; YDWDEVN; -.
DR OrthoDB; 1681738at2; -.
DR BRENDA; 5.3.1.6; 7786.
DR UniPathway; UPA00115; UER00412.
DR EvolutionaryTrace; Q7MHL9; -.
DR Proteomes; UP000002675; Chromosome I.
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 PANTHER; PTHR11934; PTHR11934; 1.
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..218
FT /note="Ribose-5-phosphate isomerase A"
FT /id="PRO_0000158494"
FT ACT_SITE 103
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 7
FT /ligand="substrate"
FT BINDING 28..31
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 81..84
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 94..97
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 121
FT /ligand="substrate"
FT HELIX 6..13
FT /evidence="ECO:0007829|PDB:3ENQ"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:3ENQ"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:3ENQ"
FT HELIX 30..40
FT /evidence="ECO:0007829|PDB:3ENQ"
FT HELIX 41..45
FT /evidence="ECO:0007829|PDB:3ENQ"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:3ENQ"
FT HELIX 54..62
FT /evidence="ECO:0007829|PDB:3ENQ"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:3ENQ"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:3ENQ"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:3ENQ"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:3ENQ"
FT HELIX 100..109
FT /evidence="ECO:0007829|PDB:3ENQ"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:3ENQ"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:3ENQ"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:3ENQ"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:3ENQ"
FT HELIX 140..149
FT /evidence="ECO:0007829|PDB:3ENQ"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:3ENQ"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:3ENQ"
FT HELIX 179..187
FT /evidence="ECO:0007829|PDB:3ENQ"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:3ENQ"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:3ENQ"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:3ENV"
SQ SEQUENCE 218 AA; 22985 MW; B5915E8097F52511 CRC64;
MTQDEMKKAA GWAALKYVEK GSIVGVGTGS TVNHFIDALG TMSEEIKGAV SSSVASTEKL
EALGIKIFDC NEVASLDIYV DGADEINADR EMIKGGGAAL TREKIVAAIA DKFICIVDGT
KAVDVLGTFP LPVEVIPMAR SYVARQLVKL GGDPCYREGV ITDNGNVILD VYGMKITNPK
QLEDQINAIP GVVTVGLFAH RGADVVITGT PEGAKIEE
