PQQB_METEA
ID PQQB_METEA Reviewed; 299 AA.
AC Q49149; C5B130;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Coenzyme PQQ synthesis protein B {ECO:0000255|HAMAP-Rule:MF_00653};
DE AltName: Full=Coenzyme PQQ synthesis protein G;
DE AltName: Full=Pyrroloquinoline quinone biosynthesis protein B {ECO:0000255|HAMAP-Rule:MF_00653};
GN Name=pqqB {ECO:0000255|HAMAP-Rule:MF_00653}; Synonyms=pqqG;
GN OrderedLocusNames=MexAM1_META1p1750;
OS Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS 9133 / AM1) (Methylobacterium extorquens).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=272630;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8132470; DOI=10.1128/jb.176.6.1746-1755.1994;
RA Morris C.J., Biville F., Turlin E., Lee E., Ellermann K., Fan W.H.,
RA Ramamoorthi R., Springer A.L., Lidstrom M.E.;
RT "Isolation, phenotypic characterization, and complementation analysis of
RT mutants of Methylobacterium extorquens AM1 unable to synthesize
RT pyrroloquinoline quinone and sequences of pqqD, pqqG, and pqqC.";
RL J. Bacteriol. 176:1746-1755(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA Lidstrom M.E.;
RT "Methylobacterium genome sequences: a reference blueprint to investigate
RT microbial metabolism of C1 compounds from natural and industrial sources.";
RL PLoS ONE 4:E5584-E5584(2009).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACS39594.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L25889; AAA17879.1; -; Unassigned_DNA.
DR EMBL; CP001510; ACS39594.1; ALT_INIT; Genomic_DNA.
DR PIR; B55527; B55527.
DR RefSeq; WP_003597599.1; NC_012808.1.
DR PDB; 4Z7R; X-ray; 1.98 A; A/B=1-299.
DR PDBsum; 4Z7R; -.
DR AlphaFoldDB; Q49149; -.
DR SMR; Q49149; -.
DR STRING; 272630.MexAM1_META1p1750; -.
DR EnsemblBacteria; ACS39594; ACS39594; MexAM1_META1p1750.
DR KEGG; mea:Mex_1p1750; -.
DR eggNOG; COG1235; Bacteria.
DR HOGENOM; CLU_061120_0_0_5; -.
DR OrthoDB; 1712770at2; -.
DR UniPathway; UPA00539; -.
DR Proteomes; UP000009081; 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; Transport.
FT CHAIN 1..299
FT /note="Coenzyme PQQ synthesis protein B"
FT /id="PRO_0000220001"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:4Z7R"
FT HELIX 22..29
FT /evidence="ECO:0007829|PDB:4Z7R"
FT STRAND 39..54
FT /evidence="ECO:0007829|PDB:4Z7R"
FT HELIX 60..66
FT /evidence="ECO:0007829|PDB:4Z7R"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:4Z7R"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:4Z7R"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:4Z7R"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:4Z7R"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:4Z7R"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:4Z7R"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:4Z7R"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:4Z7R"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:4Z7R"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:4Z7R"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:4Z7R"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:4Z7R"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:4Z7R"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:4Z7R"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:4Z7R"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:4Z7R"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:4Z7R"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:4Z7R"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:4Z7R"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:4Z7R"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:4Z7R"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:4Z7R"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:4Z7R"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:4Z7R"
FT STRAND 259..266
FT /evidence="ECO:0007829|PDB:4Z7R"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:4Z7R"
FT HELIX 278..285
FT /evidence="ECO:0007829|PDB:4Z7R"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:4Z7R"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:4Z7R"
SQ SEQUENCE 299 AA; 32166 MW; 8506C705EC9BA56C CRC64;
MHVVILGSAA GGGVPQWNCR CSICSLAWAG DSRVRPRTQS SIAVSPDGER WLLLNASPDI
RQQIQANPQM HPREGLRHSP IHAVLLTNGD VDHVAGLLTL REGQPFTLYA TPGILASVSD
NRVFDVMAAD VVKRQTIALN ETFEPVPGLS VTLFSVPGKV PLWLEDASME IGAETETTVG
TMIEAGGKRL AYIPGCARVT EDLKARIAGA DALLFDGTVL EDDDMIRAGV GTKTGWRMGH
IQMNGETGSI ASLADIEIGR RVFVHINNTN PVLIEDSYER ASVEARGWTV AHDGLTLDL
