ID A0A2Z5G637_9BACT Unreviewed; 263 AA.
AC A0A2Z5G637;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=ACPOL_5434 {ECO:0000313|EMBL:AXC14682.1};
OS Acidisarcina polymorpha.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Acidisarcina.
OX NCBI_TaxID=2211140 {ECO:0000313|EMBL:AXC14682.1, ECO:0000313|Proteomes:UP000253606};
RN [1] {ECO:0000313|EMBL:AXC14682.1, ECO:0000313|Proteomes:UP000253606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SBC82 {ECO:0000313|EMBL:AXC14682.1,
RC ECO:0000313|Proteomes:UP000253606};
RX PubMed=30510549; DOI=10.3389/fmicb.2018.02775;
RA Belova S.E., Ravin N.V., Pankratov T.A., Rakitin A.L., Ivanova A.A.,
RA Beletsky A.V., Mardanov A.V., Sinninghe Damste J.S., Dedysh S.N.;
RT "Hydrolytic Capabilities as a Key to Environmental Success: Chitinolytic
RT and Cellulolytic Acidobacteria From Acidic Sub-arctic Soils and Boreal
RT Peatlands.";
RL Front. Microbiol. 9:2775-2775(2018).
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; CP030840; AXC14682.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z5G637; -.
DR KEGG; abas:ACPOL_5434; -.
DR UniPathway; UPA00539; -.
DR Proteomes; UP000253606; Chromosome.
DR GO; GO:0018189; P:pyrroloquinoline quinone biosynthetic process; IEA:UniProtKB-UniRule.
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 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:UP000253606};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00653}.
FT DOMAIN 13..231
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF12706"
SQ SEQUENCE 263 AA; 28930 MW; 859F423C101C8C80 CRC64;
MQLQASFSGD GENWFLINAC PDLRYQIEAN PELQPSAALG KRNTPLHGIL LTSADLDQVL
GVLLLREFQP LTIYATSLVR KVLEANTFFR MLDRVPQQLT WVEISPDHPL LLDHEITCRA
IPLSGSLPFY ARDVNPAQDG QASLGLLLEA SGLRIAYTPS LPKITEELLA IYSTSDVILV
DGTFWSDAEL SSTHAGTPSA RSIGHIPMSG DDGIIALLSQ IKKPKKVFVH INNTNPVLDP
RSAEYNQVIQ AGWEIGHDGW QLN
//
