RPIA_HAEIN
ID RPIA_HAEIN Reviewed; 219 AA.
AC P44725;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 133.
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=HI_0464;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=10675023;
RX DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4;
RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C.,
RA Fountoulakis M.;
RT "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL Electrophoresis 21:411-429(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, AND
RP SUBUNIT.
RA Das K., Xiao R., Acton T., Montelione G., Arnold E.;
RT "D-ribose-5-phosphate isomerase, IR21.";
RL Submitted (JUN-2002) 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.3}.
CC -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00170}.
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DR EMBL; L42023; AAC22123.1; -; Genomic_DNA.
DR PIR; B64153; B64153.
DR RefSeq; NP_438625.1; NC_000907.1.
DR RefSeq; WP_005693699.1; NC_000907.1.
DR PDB; 1M0S; X-ray; 1.90 A; A/B=1-219.
DR PDBsum; 1M0S; -.
DR AlphaFoldDB; P44725; -.
DR SMR; P44725; -.
DR STRING; 71421.HI_0464; -.
DR DrugBank; DB04272; Citric acid.
DR EnsemblBacteria; AAC22123; AAC22123; HI_0464.
DR KEGG; hin:HI_0464; -.
DR PATRIC; fig|71421.8.peg.484; -.
DR eggNOG; COG0120; Bacteria.
DR HOGENOM; CLU_056590_1_1_6; -.
DR OMA; YDWDEVN; -.
DR PhylomeDB; P44725; -.
DR BioCyc; HINF71421:G1GJ1-480-MON; -.
DR UniPathway; UPA00115; UER00412.
DR EvolutionaryTrace; P44725; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IBA:GO_Central.
DR GO; GO:0006014; P:D-ribose metabolic process; IBA:GO_Central.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IBA:GO_Central.
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..219
FT /note="Ribose-5-phosphate isomerase A"
FT /id="PRO_0000158423"
FT ACT_SITE 103
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 28..31
FT /ligand="substrate"
FT BINDING 81..84
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 94..97
FT /ligand="substrate"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT HELIX 3..14
FT /evidence="ECO:0007829|PDB:1M0S"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:1M0S"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:1M0S"
FT HELIX 30..40
FT /evidence="ECO:0007829|PDB:1M0S"
FT HELIX 41..45
FT /evidence="ECO:0007829|PDB:1M0S"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:1M0S"
FT HELIX 54..62
FT /evidence="ECO:0007829|PDB:1M0S"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:1M0S"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:1M0S"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:1M0S"
FT HELIX 100..109
FT /evidence="ECO:0007829|PDB:1M0S"
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:1M0S"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:1M0S"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1M0S"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:1M0S"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:1M0S"
FT HELIX 141..150
FT /evidence="ECO:0007829|PDB:1M0S"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:1M0S"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:1M0S"
FT HELIX 180..188
FT /evidence="ECO:0007829|PDB:1M0S"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:1M0S"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:1M0S"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:1M0S"
SQ SEQUENCE 219 AA; 23094 MW; BB8ABD085BADA3C1 CRC64;
MNQLEMKKLA AQAALQYVKA DTIVGVGSGS TVNCFIEALG TIKDKIQGAV AASKESEELL
RKQGIEVFNA NDVSSLDIYV DGADEINPQK MMIKGGGAAL TREKIVAALA KKFICIVDSS
KQVDVLGSTF PLPVEVIPMA RSQVGRKLAA LGGSPEYREG VVTDNGNVIL DVHNFSILNP
VEIEKELNNV AGVVTNGIFA LRGADVVIVG TPEGAKVID
