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RPIA_NEIG2
ID   RPIA_NEIG2              Reviewed;         223 AA.
AC   B4RL16;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=NGK_0826;
OS   Neisseria gonorrhoeae (strain NCCP11945).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=521006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCCP11945;
RX   PubMed=18586945; DOI=10.1128/jb.00566-08;
RA   Chung G.T., Yoo J.S., Oh H.B., Lee Y.S., Cha S.H., Kim S.J., Yoo C.K.;
RT   "Complete genome sequence of Neisseria gonorrhoeae NCCP11945.";
RL   J. Bacteriol. 190:6035-6036(2008).
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   -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00170}.
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DR   EMBL; CP001050; ACF29507.1; -; Genomic_DNA.
DR   RefSeq; WP_003688327.1; NC_011035.1.
DR   PDB; 5UF2; X-ray; 1.40 A; A=1-223.
DR   PDBsum; 5UF2; -.
DR   AlphaFoldDB; B4RL16; -.
DR   SMR; B4RL16; -.
DR   EnsemblBacteria; ACF29507; ACF29507; NGK_0826.
DR   GeneID; 66753291; -.
DR   KEGG; ngk:NGK_0826; -.
DR   HOGENOM; CLU_056590_1_1_4; -.
DR   OMA; YDWDEVN; -.
DR   OrthoDB; 1681738at2; -.
DR   UniPathway; UPA00115; UER00412.
DR   Proteomes; UP000002564; 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   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.
FT   CHAIN           1..223
FT                   /note="Ribose-5-phosphate isomerase A"
FT                   /id="PRO_1000097678"
FT   ACT_SITE        104
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         29..32
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           4..15
FT                   /evidence="ECO:0007829|PDB:5UF2"
FT   HELIX           16..18
FT                   /evidence="ECO:0007829|PDB:5UF2"
FT   STRAND          23..27
FT                   /evidence="ECO:0007829|PDB:5UF2"
FT   HELIX           31..43
FT                   /evidence="ECO:0007829|PDB:5UF2"
FT   STRAND          48..54
FT                   /evidence="ECO:0007829|PDB:5UF2"
FT   HELIX           55..63
FT                   /evidence="ECO:0007829|PDB:5UF2"
FT   HELIX           71..73
FT                   /evidence="ECO:0007829|PDB:5UF2"
FT   STRAND          77..82
FT                   /evidence="ECO:0007829|PDB:5UF2"
FT   STRAND          85..87
FT                   /evidence="ECO:0007829|PDB:5UF2"
FT   HELIX           101..109
FT                   /evidence="ECO:0007829|PDB:5UF2"
FT   STRAND          114..119
FT                   /evidence="ECO:0007829|PDB:5UF2"
FT   HELIX           120..122
FT                   /evidence="ECO:0007829|PDB:5UF2"
FT   STRAND          125..127
FT                   /evidence="ECO:0007829|PDB:5UF2"
FT   STRAND          132..136
FT                   /evidence="ECO:0007829|PDB:5UF2"
FT   HELIX           138..140
FT                   /evidence="ECO:0007829|PDB:5UF2"
FT   HELIX           141..151
FT                   /evidence="ECO:0007829|PDB:5UF2"
FT   STRAND          154..157
FT                   /evidence="ECO:0007829|PDB:5UF2"
FT   STRAND          168..174
FT                   /evidence="ECO:0007829|PDB:5UF2"
FT   HELIX           180..188
FT                   /evidence="ECO:0007829|PDB:5UF2"
FT   STRAND          193..200
FT                   /evidence="ECO:0007829|PDB:5UF2"
FT   STRAND          205..211
FT                   /evidence="ECO:0007829|PDB:5UF2"
FT   STRAND          214..218
FT                   /evidence="ECO:0007829|PDB:5UF2"
SQ   SEQUENCE   223 AA;  23890 MW;  4F781726C0F0B73F CRC64;
     MTTQDELKRI AAEKAVEFVP ENEYIGIGTG STINFFIEAL GKSGKKIKGA VSTSKKSGEL
     LARYDIPVVS LNEVSGLAVY IDGADEVNHA LQMIKGGGGA HLNEKIVASA SEKFVCIADE
     SKYVSRLGKF PLPVEAVESA RSLVSRKLLA MGGQPELRIG YTTFYGNQIV DVHGLNIDQP
     LTMEDEINKI TGVLENGIFA RDAADVLILG TEEGAKVIYP CQG
 
 
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