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UBIC_ALBFT
ID   UBIC_ALBFT              Reviewed;         197 AA.
AC   Q21U27;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=Rfer_3015;
OS   Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS   (Rhodoferax ferrireducens).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=338969;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-621 / DSM 15236 / T118;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000267; ABD70726.1; -; Genomic_DNA.
DR   RefSeq; WP_011465292.1; NC_007908.1.
DR   AlphaFoldDB; Q21U27; -.
DR   SMR; Q21U27; -.
DR   STRING; 338969.Rfer_3015; -.
DR   EnsemblBacteria; ABD70726; ABD70726; Rfer_3015.
DR   KEGG; rfr:Rfer_3015; -.
DR   eggNOG; COG3161; Bacteria.
DR   HOGENOM; CLU_096824_2_0_4; -.
DR   OMA; HTIVHPR; -.
DR   OrthoDB; 1274776at2; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000008332; Chromosome.
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..197
FT                   /note="Probable chorismate pyruvate-lyase"
FT                   /id="PRO_0000255912"
FT   BINDING         66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
FT   BINDING         104
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
SQ   SEQUENCE   197 AA;  21319 MW;  ED0DA6E7F7DA36EB CRC64;
     MKVWSKRNVQ RGNRKRWVGA TGSLSARLAA AGQRFSVQVL SQGLQALDPD EASALGLSRL
     KVGYVREVLL RVDEVAVVFA RSVTAHPHSQ GPWRSIRGLG TRPLADVLFG QHGIARTPLQ
     FASLQVASSL HRHVAHAWLG ATGAALASRV LPARRSVFTR GAAPLLVMEV FAAPHAPWGW
     LTTKTRRGPP ALPRTKP
 
 
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