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UBIC_PHOPR
ID   UBIC_PHOPR              Reviewed;         180 AA.
AC   Q6LVS4;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Probable chorismate pyruvate-lyase {ECO:0000255|HAMAP-Rule:MF_01632};
DE            Short=CL {ECO:0000255|HAMAP-Rule:MF_01632};
DE            Short=CPL {ECO:0000255|HAMAP-Rule:MF_01632};
DE            EC=4.1.3.40 {ECO:0000255|HAMAP-Rule:MF_01632};
GN   Name=ubiC {ECO:0000255|HAMAP-Rule:MF_01632}; OrderedLocusNames=PBPRA0162;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
CC   -!- FUNCTION: Removes the pyruvyl group from chorismate, with concomitant
CC       aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the
CC       ubiquinone pathway. {ECO:0000255|HAMAP-Rule:MF_01632}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chorismate = 4-hydroxybenzoate + pyruvate;
CC         Xref=Rhea:RHEA:16505, ChEBI:CHEBI:15361, ChEBI:CHEBI:17879,
CC         ChEBI:CHEBI:29748; EC=4.1.3.40; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01632};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01632}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01632}.
CC   -!- SIMILARITY: Belongs to the UbiC family. {ECO:0000255|HAMAP-
CC       Rule:MF_01632}.
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DR   EMBL; CR378663; CAG18601.1; -; Genomic_DNA.
DR   RefSeq; WP_011216979.1; NC_006370.1.
DR   AlphaFoldDB; Q6LVS4; -.
DR   SMR; Q6LVS4; -.
DR   STRING; 298386.PBPRA0162; -.
DR   PRIDE; Q6LVS4; -.
DR   EnsemblBacteria; CAG18601; CAG18601; PBPRA0162.
DR   KEGG; ppr:PBPRA0162; -.
DR   eggNOG; COG3161; Bacteria.
DR   HOGENOM; CLU_096824_1_1_6; -.
DR   OMA; ELWGRRS; -.
DR   OrthoDB; 1274776at2; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000000593; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008813; F:chorismate lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042866; P:pyruvate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1410.10; -; 1.
DR   HAMAP; MF_01632; UbiC; 1.
DR   InterPro; IPR007440; Chorismate--pyruvate_lyase.
DR   InterPro; IPR028978; Chorismate_lyase_/UTRA_dom_sf.
DR   PANTHER; PTHR38683; PTHR38683; 1.
DR   Pfam; PF04345; Chor_lyase; 1.
DR   SUPFAM; SSF64288; SSF64288; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Lyase; Pyruvate; Reference proteome; Ubiquinone biosynthesis.
FT   CHAIN           1..180
FT                   /note="Probable chorismate pyruvate-lyase"
FT                   /id="PRO_0000240552"
FT   BINDING         82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
SQ   SEQUENCE   180 AA;  20515 MW;  ADB8B8573D2FEF16 CRC64;
     MSKFKQLYKP LLDNAQWETP LSLAIEGTAF GHWLLEPNSL SRRLQRHCDE FTVSLIEQKK
     IDSTMLSADE RELIGDVDCL LRKVVLMGDG QPWVFARTLI PLSTLTGQES DLEQLGEMPL
     GFRVFTDRSA RRDALEVANT GTQAQPLWAR RSRLWINNKP LLVAELFLAQ APVYSKEKQC
 
 
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