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RPIA_METJA
ID   RPIA_METJA              Reviewed;         226 AA.
AC   Q58998;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 130.
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=MJ1603;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   PATHWAY.
RX   PubMed=16237021; DOI=10.1128/jb.187.21.7382-7389.2005;
RA   Grochowski L.L., Xu H., White R.H.;
RT   "Ribose-5-phosphate biosynthesis in Methanocaldococcus jannaschii occurs in
RT   the absence of a pentose-phosphate pathway.";
RL   J. Bacteriol. 187:7382-7389(2005).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP   ACTIVE SITE, AND SUBUNIT.
RX   PubMed=20054114; DOI=10.1107/s1744309109044923;
RA   Strange R.W., Antonyuk S.V., Ellis M.J., Bessho Y., Kuramitsu S.,
RA   Yokoyama S., Hasnain S.S.;
RT   "The structure of an archaeal ribose-5-phosphate isomerase from
RT   Methanocaldococcus jannaschii (MJ1603).";
RL   Acta Crystallogr. F 65:1214-1217(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 biosynthesis; D-ribose 5-phosphate biosynthesis.
CC       {ECO:0000269|PubMed:16237021}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:20054114}.
CC   -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00170}.
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DR   EMBL; L77117; AAB99623.1; -; Genomic_DNA.
DR   PIR; B64500; B64500.
DR   RefSeq; WP_010871128.1; NC_000909.1.
DR   PDB; 3IXQ; X-ray; 1.78 A; A/B/C/D=1-226.
DR   PDBsum; 3IXQ; -.
DR   AlphaFoldDB; Q58998; -.
DR   SMR; Q58998; -.
DR   STRING; 243232.MJ_1603; -.
DR   EnsemblBacteria; AAB99623; AAB99623; MJ_1603.
DR   GeneID; 1452512; -.
DR   KEGG; mja:MJ_1603; -.
DR   eggNOG; arCOG01122; Archaea.
DR   HOGENOM; CLU_056590_1_1_2; -.
DR   InParanoid; Q58998; -.
DR   OMA; YDWDEVN; -.
DR   OrthoDB; 98657at2157; -.
DR   PhylomeDB; Q58998; -.
DR   BRENDA; 5.3.1.6; 3260.
DR   UniPathway; UPA00293; -.
DR   EvolutionaryTrace; Q58998; -.
DR   Proteomes; UP000000805; 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; IDA:UniProtKB.
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; Carbohydrate metabolism; Isomerase; Reference proteome.
FT   CHAIN           1..226
FT                   /note="Ribose-5-phosphate isomerase A"
FT                   /id="PRO_0000158510"
FT   ACT_SITE        106
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000305|PubMed:20054114"
FT   BINDING         28..31
FT                   /ligand="substrate"
FT   BINDING         83..86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305"
FT   BINDING         97..100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305"
FT   BINDING         124
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   HELIX           4..14
FT                   /evidence="ECO:0007829|PDB:3IXQ"
FT   HELIX           15..17
FT                   /evidence="ECO:0007829|PDB:3IXQ"
FT   STRAND          23..26
FT                   /evidence="ECO:0007829|PDB:3IXQ"
FT   HELIX           30..46
FT                   /evidence="ECO:0007829|PDB:3IXQ"
FT   STRAND          51..56
FT                   /evidence="ECO:0007829|PDB:3IXQ"
FT   HELIX           57..65
FT                   /evidence="ECO:0007829|PDB:3IXQ"
FT   TURN            73..75
FT                   /evidence="ECO:0007829|PDB:3IXQ"
FT   STRAND          79..83
FT                   /evidence="ECO:0007829|PDB:3IXQ"
FT   STRAND          86..89
FT                   /evidence="ECO:0007829|PDB:3IXQ"
FT   TURN            90..92
FT                   /evidence="ECO:0007829|PDB:3IXQ"
FT   HELIX           103..112
FT                   /evidence="ECO:0007829|PDB:3IXQ"
FT   STRAND          113..121
FT                   /evidence="ECO:0007829|PDB:3IXQ"
FT   HELIX           122..124
FT                   /evidence="ECO:0007829|PDB:3IXQ"
FT   STRAND          125..128
FT                   /evidence="ECO:0007829|PDB:3IXQ"
FT   STRAND          131..133
FT                   /evidence="ECO:0007829|PDB:3IXQ"
FT   STRAND          135..139
FT                   /evidence="ECO:0007829|PDB:3IXQ"
FT   HELIX           141..143
FT                   /evidence="ECO:0007829|PDB:3IXQ"
FT   HELIX           144..153
FT                   /evidence="ECO:0007829|PDB:3IXQ"
FT   STRAND          157..160
FT                   /evidence="ECO:0007829|PDB:3IXQ"
FT   STRAND          164..169
FT                   /evidence="ECO:0007829|PDB:3IXQ"
FT   STRAND          177..182
FT                   /evidence="ECO:0007829|PDB:3IXQ"
FT   HELIX           188..196
FT                   /evidence="ECO:0007829|PDB:3IXQ"
FT   STRAND          201..207
FT                   /evidence="ECO:0007829|PDB:3IXQ"
FT   STRAND          211..217
FT                   /evidence="ECO:0007829|PDB:3IXQ"
FT   STRAND          220..224
FT                   /evidence="ECO:0007829|PDB:3IXQ"
SQ   SEQUENCE   226 AA;  24830 MW;  C0F1C2C1A5499123 CRC64;
     MSNEDLKLKV AKEAVKLVKD GMVIGLGTGS TAALFIRELG NRIREEELTV FGIPTSFEAK
     MLAMQYEIPL VTLDEYDVDI AFDGADEVEE TTLFLIKGGG GCHTQEKIVD YNANEFVVLV
     DESKLVKKLG EKFPIPVEVI PSAYRVVIRA LSEMGGEAVI RLGDRKRGPV ITDNGNMIID
     VFMNIDDAIE LEKEINNIPG VVENGIFTKV DKVLVGTKKG VKTLKK
 
 
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