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Database: UniProt
Entry: A0A1D9H9L9_9BURK
LinkDB: A0A1D9H9L9_9BURK
Original site: A0A1D9H9L9_9BURK 
ID   A0A1D9H9L9_9BURK        Unreviewed;       305 AA.
AC   A0A1D9H9L9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Coenzyme PQQ synthesis protein B {ECO:0000256|ARBA:ARBA00015084, ECO:0000256|HAMAP-Rule:MF_00653};
DE   AltName: Full=Pyrroloquinoline quinone biosynthesis protein B {ECO:0000256|HAMAP-Rule:MF_00653};
GN   Name=pqqB {ECO:0000256|HAMAP-Rule:MF_00653};
GN   ORFNames=BKK79_34055 {ECO:0000313|EMBL:AOY96561.1};
OS   Cupriavidus sp. USMAA2-4.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=876364 {ECO:0000313|EMBL:AOY96561.1, ECO:0000313|Proteomes:UP000178101};
RN   [1] {ECO:0000313|EMBL:AOY96561.1, ECO:0000313|Proteomes:UP000178101}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USMAA2-4 {ECO:0000313|EMBL:AOY96561.1,
RC   ECO:0000313|Proteomes:UP000178101};
RA   Abdullah A.A.-A., Shafie N.A.H., Lau N.S.;
RT   "Complete genome sequences of three Cupriavidus strains isolated from
RT   various Malaysian environments.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in the transport of PQQ or its precursor to
CC       the periplasm. {ECO:0000256|HAMAP-Rule:MF_00653}.
CC   -!- PATHWAY: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004886, ECO:0000256|HAMAP-Rule:MF_00653}.
CC   -!- SIMILARITY: Belongs to the PqqB family. {ECO:0000256|ARBA:ARBA00008481,
CC       ECO:0000256|HAMAP-Rule:MF_00653}.
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DR   EMBL; CP017749; AOY96561.1; -; Genomic_DNA.
DR   RefSeq; WP_071040045.1; NZ_CP017749.1.
DR   AlphaFoldDB; A0A1D9H9L9; -.
DR   STRING; 876364.BKK79_34055; -.
DR   KEGG; cuu:BKK79_34055; -.
DR   UniPathway; UPA00539; -.
DR   Proteomes; UP000178101; Chromosome 2.
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; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 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   NCBIfam; TIGR02108; PQQ_syn_pqqB; 1.
DR   PANTHER; PTHR42663:SF7; COENZYME PQQ SYNTHESIS PROTEIN B; 1.
DR   PANTHER; PTHR42663; HYDROLASE C777.06C-RELATED-RELATED; 1.
DR   Pfam; PF12706; Lactamase_B_2; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE   3: Inferred from homology;
KW   PQQ biosynthesis {ECO:0000256|ARBA:ARBA00022905, ECO:0000256|HAMAP-
KW   Rule:MF_00653}; Reference proteome {ECO:0000313|Proteomes:UP000178101};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00653}.
FT   DOMAIN          52..272
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|Pfam:PF12706"
SQ   SEQUENCE   305 AA;  32673 MW;  8329A9C98D26F884 CRC64;
     MVTLRVLGSA AGGGFPQWNC NCPNCAGVRR GTVRATPRTQ SSIALSENGS DWLLVNASPD
     ILAQVRATPA LQPARSQRDS GIAAVLLMDA QIDHVTGLLM LREHGRPLPL YATAPVLADL
     DQAFPLRRIL SHYCGLEAHP LPLDGSALRL AALPSLALTP VPLDSKAPPY SPNREAPQHG
     DNIGLRVVDT RSGARLFYAP GLGAIEPHVM AELQAADVVL VDGTFWQDDE MPKLGLSAKR
     ARDMGHLAQS GPGGMIEVLD AVPRARKILI HINNTNPILD EDSPQRRRLA AHGIEVAWDG
     MEIAL
//
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