ID A0A7W8E0Q6_9BRAD Unreviewed; 258 AA.
AC A0A7W8E0Q6;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 02-APR-2025, entry version 15.
DE RecName: Full=Pyrroloquinoline-quinone synthase {ECO:0000256|HAMAP-Rule:MF_00654};
DE EC=1.3.3.11 {ECO:0000256|HAMAP-Rule:MF_00654};
DE AltName: Full=Coenzyme PQQ synthesis protein C {ECO:0000256|HAMAP-Rule:MF_00654};
DE AltName: Full=Pyrroloquinoline quinone biosynthesis protein C {ECO:0000256|HAMAP-Rule:MF_00654};
GN Name=pqqC {ECO:0000256|HAMAP-Rule:MF_00654};
GN ORFNames=HNR60_003904 {ECO:0000313|EMBL:MBB5049130.1};
OS Rhodopseudomonas rhenobacensis.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Hyphomicrobiales; Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=87461 {ECO:0000313|EMBL:MBB5049130.1, ECO:0000313|Proteomes:UP000542353};
RN [1] {ECO:0000313|EMBL:MBB5049130.1, ECO:0000313|Proteomes:UP000542353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12706 {ECO:0000313|EMBL:MBB5049130.1,
RC ECO:0000313|Proteomes:UP000542353};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ring cyclization and eight-electron oxidation of 3a-(2-amino-
CC 2-carboxyethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline-7,9-
CC dicarboxylic-acid to PQQ. {ECO:0000256|HAMAP-Rule:MF_00654}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,7,8-
CC hexahydroquinoline-2,4-dicarboxylate + 3 O2 = pyrroloquinoline
CC quinone + 2 H2O2 + 2 H2O + H(+); Xref=Rhea:RHEA:10692,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:58442, ChEBI:CHEBI:58778; EC=1.3.3.11;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00654};
CC -!- PATHWAY: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00654}.
CC -!- SIMILARITY: Belongs to the PqqC family. {ECO:0000256|HAMAP-
CC Rule:MF_00654}.
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:MBB5049130.1}.
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DR EMBL; JACHIH010000031; MBB5049130.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7W8E0Q6; -.
DR UniPathway; UPA00539; -.
DR Proteomes; UP000542353; Unassembled WGS sequence.
DR GO; GO:0033732; F:pyrroloquinoline-quinone synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0018189; P:pyrroloquinoline quinone biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006790; P:sulfur compound metabolic process; IEA:UniProtKB-ARBA.
DR Gene3D; 1.20.910.10; Heme oxygenase-like; 1.
DR HAMAP; MF_00654; PQQ_syn_PqqC; 1.
DR InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR InterPro; IPR011845; PqqC.
DR InterPro; IPR039068; PqqC-like.
DR InterPro; IPR004305; Thiaminase-2/PQQC.
DR NCBIfam; TIGR02111; PQQ_syn_pqqC; 1.
DR PANTHER; PTHR40279:SF3; 4-AMINOBENZOATE SYNTHASE; 1.
DR PANTHER; PTHR40279; PQQC-LIKE PROTEIN; 1.
DR Pfam; PF03070; TENA_THI-4; 1.
DR SUPFAM; SSF48613; Heme oxygenase-like; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00654};
KW PQQ biosynthesis {ECO:0000256|ARBA:ARBA00022905, ECO:0000256|HAMAP-
KW Rule:MF_00654}; Reference proteome {ECO:0000313|Proteomes:UP000542353}.
FT DOMAIN 27..237
FT /note="Thiaminase-2/PQQC"
FT /evidence="ECO:0000259|Pfam:PF03070"
SQ SEQUENCE 258 AA; 29080 MW; CD26E95AE419F257 CRC64;
MNAPLYGMSA FSLATTTRLQ DADQLEAALR QIGATRYHNL HPFHRLLHGG KLNKGQVQAW
ALNRYYYQCS IPIKDAVVIS RFSDRATRVE WRHRLEDHDG DLGAEGGIER WLKLTDGLGL
DSAYVESTQG ILPATRFAVD AYVHFVRDKS PLEAIASSLT ELFAPNLHEE RIAGMLEHYD
FVNPQIMSYF KRRLTQAPRD AQFALTYVKR HAGTPAEREA VCNALIFKTN VLWAQLDALH
HAYVDGHIPP GAFVPEAN
//
