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PQQB_RUEPO
ID   PQQB_RUEPO              Reviewed;         295 AA.
AC   Q5LTB1;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Coenzyme PQQ synthesis protein B;
DE   AltName: Full=Pyrroloquinoline quinone biosynthesis protein B;
GN   Name=pqqB; OrderedLocusNames=SPO1503;
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: May be involved in the transport of PQQ or its precursor to
CC       the periplasm, in association with PQQ biosynthesis, but is not
CC       absolutely required for this synthesis.
CC   -!- PATHWAY: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis.
CC   -!- SIMILARITY: Belongs to the PqqB family. {ECO:0000305}.
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DR   EMBL; CP000031; AAV94790.1; -; Genomic_DNA.
DR   RefSeq; WP_011047240.1; NC_003911.12.
DR   AlphaFoldDB; Q5LTB1; -.
DR   SMR; Q5LTB1; -.
DR   STRING; 246200.SPO1503; -.
DR   EnsemblBacteria; AAV94790; AAV94790; SPO1503.
DR   KEGG; sil:SPO1503; -.
DR   eggNOG; COG1235; Bacteria.
DR   HOGENOM; CLU_061120_0_0_5; -.
DR   OMA; FYIPGCA; -.
DR   OrthoDB; 1712770at2; -.
DR   UniPathway; UPA00539; -.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0018189; P:pyrroloquinoline quinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.60.15.10; -; 1.
DR   HAMAP; MF_00653; PQQ_syn_PqqB; 1.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR011842; PQQ_synth_PqqB.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   Pfam; PF12706; Lactamase_B_2; 1.
DR   SUPFAM; SSF56281; SSF56281; 1.
DR   TIGRFAMs; TIGR02108; PQQ_syn_pqqB; 1.
PE   3: Inferred from homology;
KW   PQQ biosynthesis; Reference proteome; Transport.
FT   CHAIN           1..295
FT                   /note="Coenzyme PQQ synthesis protein B"
FT                   /id="PRO_0000220010"
SQ   SEQUENCE   295 AA;  31570 MW;  C603B12F5AFBF0E9 CRC64;
     MKIVVLGAAA GGGLPQWNCG CVNCSDARAG RLRPSGQSSL AVSADGSRWS ILNASPDIRQ
     QMQDRSVLHP QGLRGSPVAS VLVTNGDIDH IAGLLSLREQ TPFDLFATAG IHEVLEGNRI
     FDALARDKVA RRPVALESPF ALHDGLEAML FAVPGKVPLF MEGESVDTGL IGEQTVGVRL
     SDGRNTAYYI PGCAYVPDDL LHRLSDAGHL LFDGTLWDDD EMIRSGTGIK TGRRMGHIPI
     SGPDGSLVRL AGLAADKTYI HINNTNPVWR AGSAERAELA RRGWQVAHDG LEIVL
 
 
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