ID K9NJ70_9PSED Unreviewed; 304 AA.
AC K9NJ70;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 54.
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|ARBA:ARBA00030966, ECO:0000256|HAMAP-Rule:MF_00653};
GN Name=pqqB1 {ECO:0000313|EMBL:AFY20136.1};
GN Synonyms=pqqB {ECO:0000256|HAMAP-Rule:MF_00653};
GN ORFNames=PputUW4_02941 {ECO:0000313|EMBL:AFY20136.1};
OS Pseudomonas sp. UW4.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1207075 {ECO:0000313|EMBL:AFY20136.1, ECO:0000313|Proteomes:UP000010397};
RN [1] {ECO:0000313|EMBL:AFY20136.1, ECO:0000313|Proteomes:UP000010397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UW4 {ECO:0000313|EMBL:AFY20136.1,
RC ECO:0000313|Proteomes:UP000010397};
RX PubMed=23516524;
RA Duan J., Jiang W., Cheng Z., Heikkila J.J., Glick B.R.;
RT "The Complete Genome Sequence of the Plant Growth-Promoting Bacterium
RT Pseudomonas sp. UW4.";
RL PLoS ONE 8:E58640-E58640(2013).
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; CP003880; AFY20136.1; -; Genomic_DNA.
DR RefSeq; WP_015095427.1; NC_019670.1.
DR AlphaFoldDB; K9NJ70; -.
DR STRING; 1207075.PputUW4_02941; -.
DR KEGG; ppuu:PputUW4_02941; -.
DR PATRIC; fig|1207075.3.peg.2995; -.
DR eggNOG; COG1235; Bacteria.
DR HOGENOM; CLU_061120_0_0_6; -.
DR OrthoDB; 9778305at2; -.
DR UniPathway; UPA00539; -.
DR Proteomes; UP000010397; 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; 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};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00653}.
FT DOMAIN 51..271
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF12706"
SQ SEQUENCE 304 AA; 33287 MW; D5D38CFF14B2DD0D CRC64;
MHIRVLGSAA GGGFPQWNCN CRQCAGVRNG SLRAQRRTQS SIALSDDGVE WVLCNASPDI
RAQLESFAPL QPARRLRDSA IAGIVLLDSQ IDHCTGLLSL REGCPHDVWC TERVHQDLSS
GFPLFNMLGH WNGGLQWQPV GLDRQPFGIA ACGHLQFRAI PLVSNAPPYS PNRGNPQPGD
TIGLFIEDLR SGASLFYAPG LGRIDDEVLG WMQRADCLLL DGTLWRDDEM RICEVGQSLG
SEMGHLPQSG PGGMLDVLAG FNRQRKVLIH INNTNPILDE DSAERALLER RGIEVAYDGM
SIEL
//
