PQQC_ACICJ
ID PQQC_ACICJ Reviewed; 246 AA.
AC A5FUM6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Pyrroloquinoline-quinone synthase {ECO:0000255|HAMAP-Rule:MF_00654};
DE EC=1.3.3.11 {ECO:0000255|HAMAP-Rule:MF_00654};
DE AltName: Full=Coenzyme PQQ synthesis protein C {ECO:0000255|HAMAP-Rule:MF_00654};
DE AltName: Full=Pyrroloquinoline quinone biosynthesis protein C {ECO:0000255|HAMAP-Rule:MF_00654};
GN Name=pqqC {ECO:0000255|HAMAP-Rule:MF_00654}; OrderedLocusNames=Acry_0079;
OS Acidiphilium cryptum (strain JF-5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=349163;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JF-5;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL Submitted (MAY-2007) 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:0000255|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 = H(+) + 2 H2O + 2 H2O2 +
CC pyrroloquinoline quinone; Xref=Rhea:RHEA:10692, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:58442, ChEBI:CHEBI:58778; EC=1.3.3.11;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00654};
CC -!- PATHWAY: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00654}.
CC -!- SIMILARITY: Belongs to the PqqC family. {ECO:0000255|HAMAP-
CC Rule:MF_00654}.
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DR EMBL; CP000697; ABQ29308.1; -; Genomic_DNA.
DR RefSeq; WP_007422717.1; NC_009484.1.
DR AlphaFoldDB; A5FUM6; -.
DR SMR; A5FUM6; -.
DR STRING; 349163.Acry_0079; -.
DR PRIDE; A5FUM6; -.
DR EnsemblBacteria; ABQ29308; ABQ29308; Acry_0079.
DR KEGG; acr:Acry_0079; -.
DR eggNOG; COG5424; Bacteria.
DR HOGENOM; CLU_080136_0_0_5; -.
DR OMA; YYQISIP; -.
DR OrthoDB; 1571811at2; -.
DR UniPathway; UPA00539; -.
DR Proteomes; UP000000245; Chromosome.
DR GO; GO:0033732; F:pyrroloquinoline-quinone synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:UniProt.
DR GO; GO:0018189; P:pyrroloquinoline quinone biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.910.10; -; 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 PANTHER; PTHR40279; PTHR40279; 1.
DR Pfam; PF03070; TENA_THI-4; 1.
DR SUPFAM; SSF48613; SSF48613; 1.
DR TIGRFAMs; TIGR02111; PQQ_syn_pqqC; 1.
PE 3: Inferred from homology;
KW Oxidoreductase; PQQ biosynthesis; Reference proteome.
FT CHAIN 1..246
FT /note="Pyrroloquinoline-quinone synthase"
FT /id="PRO_1000061666"
SQ SEQUENCE 246 AA; 27693 MW; 06241FA6803AA75D CRC64;
MTVLMSPDEL EAALRAVGAA RYHNRHPFHQ LLHGGKLDKR QVQAWALNRY CYQAAIPIKD
ATLIARTDDS ELRRIWRQRL VDHDGTQPGE GGIVRWLALA EGLGLDRDMV ISERRALPAT
RFAVRAYVDF VRDRSLLEAV ASSLTEMFSP TIISERVSGM LANYDFITRE TLAYFNARLD
QAPRDADFAL DYVKRHARTP EQQQAAIAAL TFKCDVLWAQ LDALHHAYVS PGLIPPGAFG
HDGIWS
