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PQQA_RUEPO
ID   PQQA_RUEPO              Reviewed;          35 AA.
AC   Q5LTB0;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Coenzyme PQQ synthesis protein A {ECO:0000255|HAMAP-Rule:MF_00656};
DE   AltName: Full=Pyrroloquinoline quinone biosynthesis protein A {ECO:0000255|HAMAP-Rule:MF_00656};
GN   Name=pqqA {ECO:0000255|HAMAP-Rule:MF_00656}; OrderedLocusNames=SPO1504;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS   pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA   Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT   environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
CC   -!- FUNCTION: Required for coenzyme pyrroloquinoline quinone (PQQ)
CC       biosynthesis. PQQ is probably formed by cross-linking a specific
CC       glutamate to a specific tyrosine residue and excising these residues
CC       from the peptide. {ECO:0000255|HAMAP-Rule:MF_00656}.
CC   -!- PATHWAY: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00656}.
CC   -!- SIMILARITY: Belongs to the PqqA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00656}.
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DR   EMBL; CP000031; AAV94791.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5LTB0; -.
DR   STRING; 246200.SPO1504; -.
DR   EnsemblBacteria; AAV94791; AAV94791; SPO1504.
DR   KEGG; sil:SPO1504; -.
DR   eggNOG; ENOG5033IYR; Bacteria.
DR   HOGENOM; CLU_219399_1_0_5; -.
DR   UniPathway; UPA00539; -.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0018189; P:pyrroloquinoline quinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00656; PQQ_syn_PqqA; 1.
DR   InterPro; IPR011725; PQQ_synth_PqqA.
DR   Pfam; PF08042; PqqA; 1.
DR   TIGRFAMs; TIGR02107; PQQ_syn_pqqA; 1.
PE   3: Inferred from homology;
KW   PQQ biosynthesis; Reference proteome.
FT   CHAIN           1..35
FT                   /note="Coenzyme PQQ synthesis protein A"
FT                   /id="PRO_0000220319"
FT   CROSSLNK        16..20
FT                   /note="Pyrroloquinoline quinone (Glu-Tyr)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00656"
SQ   SEQUENCE   35 AA;  3837 MW;  43C92D20540707CB CRC64;
     MAWTAPKLRE VNCGMEINMY APAEDEGGRG TDPIL
 
 
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