PQQB_PSEPK
ID PQQB_PSEPK Reviewed; 303 AA.
AC Q88QV5;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Coenzyme PQQ synthesis protein B {ECO:0000255|HAMAP-Rule:MF_00653};
DE AltName: Full=Pyrroloquinoline quinone biosynthesis protein B {ECO:0000255|HAMAP-Rule:MF_00653};
GN Name=pqqB {ECO:0000255|HAMAP-Rule:MF_00653}; OrderedLocusNames=PP_0379;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
CC -!- FUNCTION: May be involved in the transport of PQQ or its precursor to
CC the periplasm. {ECO:0000255|HAMAP-Rule:MF_00653}.
CC -!- PATHWAY: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00653}.
CC -!- SIMILARITY: Belongs to the PqqB family. {ECO:0000255|HAMAP-
CC Rule:MF_00653}.
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DR EMBL; AE015451; AAN66010.1; -; Genomic_DNA.
DR RefSeq; NP_742546.1; NC_002947.4.
DR RefSeq; WP_010951729.1; NC_002947.4.
DR PDB; 1XTO; X-ray; 2.80 A; A=1-303.
DR PDB; 3JXP; X-ray; 2.20 A; A=1-303.
DR PDB; 4Z5Y; X-ray; 1.56 A; A=1-303.
DR PDB; 4Z5Z; X-ray; 2.54 A; A=1-303.
DR PDB; 4Z60; X-ray; 2.50 A; A=1-303.
DR PDB; 4Z67; X-ray; 1.50 A; A=1-303.
DR PDB; 4Z6X; X-ray; 1.68 A; A=1-303.
DR PDB; 6E13; X-ray; 2.35 A; A=1-303.
DR PDBsum; 1XTO; -.
DR PDBsum; 3JXP; -.
DR PDBsum; 4Z5Y; -.
DR PDBsum; 4Z5Z; -.
DR PDBsum; 4Z60; -.
DR PDBsum; 4Z67; -.
DR PDBsum; 4Z6X; -.
DR PDBsum; 6E13; -.
DR AlphaFoldDB; Q88QV5; -.
DR SMR; Q88QV5; -.
DR STRING; 160488.PP_0379; -.
DR EnsemblBacteria; AAN66010; AAN66010; PP_0379.
DR KEGG; ppu:PP_0379; -.
DR PATRIC; fig|160488.4.peg.409; -.
DR eggNOG; COG1235; Bacteria.
DR HOGENOM; CLU_061120_0_0_6; -.
DR OMA; FYIPGCA; -.
DR PhylomeDB; Q88QV5; -.
DR BioCyc; PPUT160488:G1G01-414-MON; -.
DR UniPathway; UPA00539; -.
DR EvolutionaryTrace; Q88QV5; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0018189; P:pyrroloquinoline quinone biosynthetic process; IEA:UniProtKB-UniRule.
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 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 1: Evidence at protein level;
KW 3D-structure; PQQ biosynthesis; Reference proteome; Transport.
FT CHAIN 1..303
FT /note="Coenzyme PQQ synthesis protein B"
FT /id="PRO_0000220005"
FT STRAND 1..7
FT /evidence="ECO:0007829|PDB:4Z67"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:4Z67"
FT TURN 15..18
FT /evidence="ECO:0007829|PDB:4Z67"
FT HELIX 22..28
FT /evidence="ECO:0007829|PDB:4Z67"
FT STRAND 39..55
FT /evidence="ECO:0007829|PDB:4Z67"
FT HELIX 60..65
FT /evidence="ECO:0007829|PDB:4Z67"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:4Z67"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:4Z67"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:4Z67"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:4Z67"
FT HELIX 95..103
FT /evidence="ECO:0007829|PDB:4Z67"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:4Z67"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:4Z67"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:4Z67"
FT HELIX 124..128
FT /evidence="ECO:0007829|PDB:4Z67"
FT TURN 129..133
FT /evidence="ECO:0007829|PDB:4Z67"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:4Z67"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:4Z67"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:4Z67"
FT TURN 170..173
FT /evidence="ECO:0007829|PDB:4Z67"
FT STRAND 179..187
FT /evidence="ECO:0007829|PDB:4Z67"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:4Z67"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:4Z67"
FT HELIX 205..212
FT /evidence="ECO:0007829|PDB:4Z67"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:4Z67"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:4Z67"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:4Z67"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:4Z67"
FT HELIX 253..257
FT /evidence="ECO:0007829|PDB:4Z67"
FT STRAND 263..270
FT /evidence="ECO:0007829|PDB:4Z67"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:4Z67"
FT HELIX 282..289
FT /evidence="ECO:0007829|PDB:4Z67"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:4Z67"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:4Z67"
SQ SEQUENCE 303 AA; 33331 MW; 37A3653C6B52B01E CRC64;
MYIQVLGSAA GGGFPQWNCN CVNCKGYRDG TLKATARTQS SIALSDDGVH WILCNASPDI
RAQLQAFAPM QPARALRDTG INAIVLLDSQ IDHTTGLLSL REGCPHQVWC TDMVHQDLTT
GFPLFNMLSH WNGGLQWNRI ELEGSFVIDA CPNLKFTPFP LRSAAPPYSP HRFDPHPGDN
LGLMVEDTRT GGKLFYAPGL GQVDEKLLAM MHGADCLLVD GTLWEDDEMQ RRGVGTRTGR
EMGHLAQNGP GGMLEVLDGF PRQRKVLIHI NNTNPILDEN SPERAEVLRR GVEVAFDGMS
IEL
