(data stored in ACNUC7421 zone)

SWISSPROT: Q13QW8_PARXL

ID   Q13QW8_PARXL            Unreviewed;       407 AA.
AC   Q13QW8;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   07-JUN-2017, entry version 76.
DE   RecName: Full=Coenzyme PQQ synthesis protein E {ECO:0000256|HAMAP-Rule:MF_00660};
DE   AltName: Full=Pyrroloquinoline quinone biosynthesis protein E {ECO:0000256|HAMAP-Rule:MF_00660};
GN   Name=pqqE {ECO:0000256|HAMAP-Rule:MF_00660,
GN   ECO:0000313|EMBL:ABE33521.1};
GN   ORFNames=Bxe_B2470 {ECO:0000313|EMBL:ABE33521.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33521.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33521.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33521.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00660};
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000256|HAMAP-Rule:MF_00660};
CC   -!- PATHWAY: Cofactor biosynthesis; pyrroloquinoline quinone
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00660}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. PqqE family.
CC       {ECO:0000256|HAMAP-Rule:MF_00660}.
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DR   EMBL; CP000271; ABE33521.1; -; Genomic_DNA.
DR   RefSeq; WP_011490888.1; NZ_CP008762.1.
DR   ProteinModelPortal; Q13QW8; -.
DR   STRING; 266265.Bxe_B2470; -.
DR   EnsemblBacteria; ABE33521; ABE33521; Bxe_B2470.
DR   GeneID; 4007034; -.
DR   KEGG; bxb:DR64_4797; -.
DR   KEGG; bxe:Bxe_B2470; -.
DR   PATRIC; fig|266265.5.peg.5239; -.
DR   eggNOG; ENOG4105EZY; Bacteria.
DR   eggNOG; COG0535; LUCA.
DR   HOGENOM; HOG000217923; -.
DR   KO; K06139; -.
DR   OMA; IVWNFTN; -.
DR   OrthoDB; POG091H02LS; -.
DR   UniPathway; UPA00539; -.
DR   Proteomes; UP000001817; Chromosome 2.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0018189; P:pyrroloquinoline quinone biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00660; PqqE; 1.
DR   InterPro; IPR023885; 4Fe4S-binding_SPASM_dom.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR034481; Main_SPASM_domain-containing.
DR   InterPro; IPR011843; PQQ_synth_PqqE_bac.
DR   InterPro; IPR007197; rSAM.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   Pfam; PF13186; SPASM; 1.
DR   SFLD; SFLDF00280; coenzyme_PQQ_synthesis_protein; 1.
DR   SFLD; SFLDG01386; main_SPASM_domain-containing; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR02109; PQQ_syn_pqqE; 1.
DR   TIGRFAMs; TIGR04085; rSAM_more_4Fe4S; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13QW8.
DR   SWISS-2DPAGE; Q13QW8.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00660,
KW   ECO:0000256|SAAS:SAAS00803661};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00660, ECO:0000256|SAAS:SAAS00803669};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00660,
KW   ECO:0000256|SAAS:SAAS00803637};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00660,
KW   ECO:0000256|SAAS:SAAS00803678};
KW   PQQ biosynthesis {ECO:0000256|HAMAP-Rule:MF_00660};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00660,
KW   ECO:0000256|SAAS:SAAS00803656}.
FT   DOMAIN       24    223       Elp3. {ECO:0000259|SMART:SM00729}.
FT   METAL        34     34       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_00660}.
FT   METAL        38     38       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_00660}.
FT   METAL        41     41       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_00660}.
SQ   SEQUENCE   407 AA;  44834 MW;  4F791E82142F5B0C CRC64;
     MTDLSQPGGA AQPQATPDGV APPLWLLAEL TYRCPLHCAF CYNPVDYTDH SRELSTEQWI
     GVLREARALG AAQLGFSGGE PLVRDDLEVL VGEARKLGFY TNLITSGVGL TDRRLGDLKA
     AGLDHIQLSF QDSTQELNDF LSSTRTFDLK QRVAASIKRH GFPMVLNCVL HRYNLPHVDK
     IIDMALAMGA EYLELANTQY YGWAHQNEAQ LMPTREQLEE AEAVVERYRR TQGERCKIFF
     VVPDYFERRP KRCMNGWGAV FLGVAPDGAA LPCHAARSLP GLVLPNVKET PLREIWYESD
     AFNRFRGLAW MKEPCRSCDE KERDLGGCRC QAYLLTGDAA NADPVCDKSP AHDTVVSVVN
     MARRAAAAGE AREQPILFRN DTNSRKLASA LSTAASGDTC GHGGTGG
//

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