(data stored in ACNUC7421 zone)

SWISSPROT: Q13QW5_PARXL

ID   Q13QW5_PARXL            Unreviewed;       306 AA.
AC   Q13QW5;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   30-AUG-2017, entry version 76.
DE   RecName: Full=Coenzyme PQQ synthesis protein B {ECO:0000256|HAMAP-Rule:MF_00653, ECO:0000256|SAAS:SAAS00366681};
DE   AltName: Full=Pyrroloquinoline quinone biosynthesis protein B {ECO:0000256|HAMAP-Rule:MF_00653};
GN   Name=pqqB {ECO:0000256|HAMAP-Rule:MF_00653,
GN   ECO:0000313|EMBL:ABE33524.1};
GN   ORFNames=Bxe_B2467 {ECO:0000313|EMBL:ABE33524.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33524.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33524.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33524.1,
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   -!- FUNCTION: May be involved in the transport of PQQ or its precursor
CC       to the periplasm. {ECO:0000256|HAMAP-Rule:MF_00653,
CC       ECO:0000256|SAAS:SAAS00055099}.
CC   -!- PATHWAY: Cofactor biosynthesis; pyrroloquinoline quinone
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00653,
CC       ECO:0000256|SAAS:SAAS00366676}.
CC   -!- SIMILARITY: Belongs to the PqqB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00653, ECO:0000256|SAAS:SAAS00558046}.
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DR   EMBL; CP000271; ABE33524.1; -; Genomic_DNA.
DR   RefSeq; WP_011490890.1; NZ_CP008762.1.
DR   ProteinModelPortal; Q13QW5; -.
DR   STRING; 266265.Bxe_B2467; -.
DR   EnsemblBacteria; ABE33524; ABE33524; Bxe_B2467.
DR   GeneID; 4007037; -.
DR   KEGG; bxb:DR64_4794; -.
DR   KEGG; bxe:Bxe_B2467; -.
DR   PATRIC; fig|266265.5.peg.5242; -.
DR   eggNOG; ENOG4105JIE; Bacteria.
DR   eggNOG; COG1235; LUCA.
DR   HOGENOM; HOG000217958; -.
DR   KO; K06136; -.
DR   OMA; KADCLLI; -.
DR   OrthoDB; POG091H0RX8; -.
DR   UniPathway; UPA00539; -.
DR   Proteomes; UP000001817; Chromosome 2.
DR   GO; GO:0018189; P:pyrroloquinoline quinone biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   CDD; cd16274; PQQB-like_MBL-fold; 1.
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   Pfam; PF12706; Lactamase_B_2; 1.
DR   SUPFAM; SSF56281; SSF56281; 1.
DR   TIGRFAMs; TIGR02108; PQQ_syn_pqqB; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13QW5.
DR   SWISS-2DPAGE; Q13QW5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   PQQ biosynthesis {ECO:0000256|HAMAP-Rule:MF_00653,
KW   ECO:0000256|SAAS:SAAS00055093};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_00653,
KW   ECO:0000256|SAAS:SAAS00055102}.
FT   DOMAIN       51    273       Lactamase_B. {ECO:0000259|Pfam:PF12706}.
SQ   SEQUENCE   306 AA;  32919 MW;  6F7CF2CCFBA65CFB CRC64;
     MKIKVLGSSA GGGFPQWNCN CRNCDGVRRG TIKATRRTQS SIAVSANGED WLLVNASPDL
     LAQIAANPEL QPARRARDSG IAAVLVIDAQ IDHVTGLLML RERDTPLPLY ATNAVWQDLC
     SGFPVAPILS HYCGVEHRRI ALDGAPLAID ALGGVQIDAL PLSSKAPPYS PHRNAPERGD
     NIGLVITNRQ TGKRVFYAPG LGAIEAHVLA AMREADLLLV DGTLWTADEM IRLELSKKTA
     ADMGHLQQSG PGGMIEVLDS LGAHNARKVL IHINNTNPIL VEDGPERRIL TEHGIEVAYD
     GMTFEI
//

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