ID A0A1Q6WP06_9GAMM Unreviewed; 306 AA.
AC A0A1Q6WP06;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 13-SEP-2023, entry version 18.
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=pqqB {ECO:0000256|HAMAP-Rule:MF_00653};
GN ORFNames=AUH10_02830 {ECO:0000313|EMBL:OLB14951.1};
OS Gammaproteobacteria bacterium 13_2_20CM_66_19.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1805166 {ECO:0000313|EMBL:OLB14951.1, ECO:0000313|Proteomes:UP000186999};
RN [1] {ECO:0000313|EMBL:OLB14951.1, ECO:0000313|Proteomes:UP000186999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLB14951.1}.
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DR EMBL; MNCZ01000027; OLB14951.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q6WP06; -.
DR STRING; 1805166.AUH10_02830; -.
DR UniPathway; UPA00539; -.
DR Proteomes; UP000186999; Unassembled WGS sequence.
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 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 52..272
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF12706"
SQ SEQUENCE 306 AA; 33101 MW; 6017F761C78FA1DA CRC64;
MRIRVLGSAA GGGFPQWNCN CRNCSGVRNG TLRARPRTQS SIAVSGGDER QWALVNASPD
ILAQLKANAV LQPARAPRDT AIAGIVLVDG QLDHTVGLLM LRESTRALRI WCTDPVYADL
TRGNPIFEIL AHYCGVERRE MRSDGAEFAV DGVDGLRWRA LAVTGKAAPY SPHRESPVAG
DNVALVLRDG ASGRALVYAP GLVSMDEPMW RAMQGAACVL LDGTFWSDDE MIRVGASAKR
AREIGHLPQS GPGGMLEWLE KLPAGCRRIL IHVNNTNPIL DEGSPEHAEL ARRGVEVAWD
GLEIEL
//
