PQQCD_METEA
ID PQQCD_METEA Reviewed; 372 AA.
AC Q49150; C5B129; P71518;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Bifunctional coenzyme PQQ synthesis protein C/D;
DE AltName: Full=Pyrroloquinoline quinone biosynthesis protein C/D;
DE Includes:
DE RecName: Full=Pyrroloquinoline-quinone synthase;
DE EC=1.3.3.11;
DE AltName: Full=Coenzyme PQQ synthesis protein C;
DE Includes:
DE RecName: Full=PqqA binding protein {ECO:0000303|PubMed:27638737};
DE AltName: Full=Coenzyme PQQ synthesis protein D;
GN Name=pqqCD; OrderedLocusNames=MexAM1_META1p1749;
OS Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS 9133 / AM1) (Methylobacterium extorquens).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=272630;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA Lidstrom M.E.;
RT "Methylobacterium genome sequences: a reference blueprint to investigate
RT microbial metabolism of C1 compounds from natural and industrial sources.";
RL PLoS ONE 4:E5584-E5584(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-111.
RX PubMed=8132470; DOI=10.1128/jb.176.6.1746-1755.1994;
RA Morris C.J., Biville F., Turlin E., Lee E., Ellermann K., Fan W.H.,
RA Ramamoorthi R., Springer A.L., Lidstrom M.E.;
RT "Isolation, phenotypic characterization, and complementation analysis of
RT mutants of Methylobacterium extorquens AM1 unable to synthesize
RT pyrroloquinoline quinone and sequences of pqqD, pqqG, and pqqC.";
RL J. Bacteriol. 176:1746-1755(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 110-372.
RX PubMed=9043136; DOI=10.1099/00221287-143-2-595;
RA Toyama H., Chistoserdova L., Lidstrom M.E.;
RT "Sequence analysis of pqq genes required for biosynthesis of
RT pyrroloquinoline quinone in Methylobacterium extorquens AM1 and the
RT purification of a biosynthetic intermediate.";
RL Microbiology 143:595-602(1997).
RN [4]
RP SUBUNIT, AND INTERACTION WITH PQQA AND PQQE.
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX PubMed=25817994; DOI=10.1074/jbc.m115.646521;
RA Latham J.A., Iavarone A.T., Barr I., Juthani P.V., Klinman J.P.;
RT "PqqD is a novel peptide chaperone that forms a ternary complex with the
RT radical S-adenosylmethionine protein PqqE in the pyrroloquinoline quinone
RT biosynthetic pathway.";
RL J. Biol. Chem. 290:12908-12918(2015).
RN [5]
RP FUNCTION OF PQQD REGION, SUBUNIT, AND INTERACTION WITH PQQA AND PQQE.
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX PubMed=27638737; DOI=10.1007/s12104-016-9705-8;
RA Evans R.L. III, Latham J.A., Klinman J.P., Wilmot C.M., Xia Y.;
RT "(1)H, (13)C, and (15)N resonance assignments and secondary structure
RT information for Methylobacterium extorquens PqqD and the complex of PqqD
RT with PqqA.";
RL Biomol. NMR. Assign. 10:385-389(2016).
RN [6]
RP STRUCTURE BY NMR OF 280-372, FUNCTION OF PQQD REGION, AND INTERACTION WITH
RP PQQA AND PQQE.
RX PubMed=28481092; DOI=10.1021/acs.biochem.7b00247;
RA Evans R.L. III, Latham J.A., Xia Y., Klinman J.P., Wilmot C.M.;
RT "Nuclear magnetic resonance structure and binding studies of PqqD, a
RT chaperone required in the biosynthesis of the bacterial dehydrogenase
RT cofactor pyrroloquinoline quinone.";
RL Biochemistry 56:2735-2746(2017).
CC -!- FUNCTION: The PqqC region is involved in ring cyclization and eight-
CC electron oxidation of 3a-(2-amino-2-carboxyethyl)-4,5-dioxo-
CC 4,5,6,7,8,9-hexahydroquinoline-7,9-dicarboxylic-acid to PQQ.
CC {ECO:0000250}.
CC -!- FUNCTION: The PqqD region functions as a PqqA binding domain and
CC presents PqqA to PqqE. {ECO:0000269|PubMed:27638737,
CC ECO:0000269|PubMed:28481092}.
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 -!- PATHWAY: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis.
CC -!- SUBUNIT: Monomer (PubMed:25817994, PubMed:27638737). Interacts with
CC PqqE (PubMed:25817994, PubMed:27638737, PubMed:28481092).
CC {ECO:0000269|PubMed:25817994, ECO:0000269|PubMed:27638737,
CC ECO:0000269|PubMed:28481092}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the PqqC family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PqqD family.
CC {ECO:0000305}.
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DR EMBL; CP001510; ACS39593.1; -; Genomic_DNA.
DR EMBL; L25889; AAA17880.1; -; Unassigned_DNA.
DR EMBL; U72662; AAB58899.1; -; Genomic_DNA.
DR PIR; C55527; C55527.
DR RefSeq; WP_012752611.1; NC_012808.1.
DR PDB; 5SXY; NMR; -; A=280-372.
DR PDB; 5VRC; X-ray; 2.00 A; A/B/C/D=1-260.
DR PDB; 5VRD; X-ray; 2.85 A; A/B/C/D=1-372.
DR PDBsum; 5SXY; -.
DR PDBsum; 5VRC; -.
DR PDBsum; 5VRD; -.
DR AlphaFoldDB; Q49150; -.
DR SMR; Q49150; -.
DR STRING; 272630.MexAM1_META1p1749; -.
DR EnsemblBacteria; ACS39593; ACS39593; MexAM1_META1p1749.
DR KEGG; mea:Mex_1p1749; -.
DR eggNOG; COG5424; Bacteria.
DR HOGENOM; CLU_764642_0_0_5; -.
DR OMA; AYVHFVR; -.
DR OrthoDB; 501466at2; -.
DR BRENDA; 1.3.3.11; 3296.
DR UniPathway; UPA00539; -.
DR Proteomes; UP000009081; Chromosome.
DR GO; GO:0033732; F:pyrroloquinoline-quinone synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
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; 1.10.10.1150; -; 1.
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; IPR008792; PQQD.
DR InterPro; IPR022479; PqqD_bac.
DR InterPro; IPR041881; PqqD_sf.
DR InterPro; IPR004305; Thiaminase-2/PQQC.
DR PANTHER; PTHR40279; PTHR40279; 1.
DR Pfam; PF05402; PqqD; 1.
DR Pfam; PF03070; TENA_THI-4; 1.
DR SUPFAM; SSF48613; SSF48613; 1.
DR TIGRFAMs; TIGR03859; PQQ_PqqD; 1.
DR TIGRFAMs; TIGR02111; PQQ_syn_pqqC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Oxidoreductase; PQQ biosynthesis.
FT CHAIN 1..372
FT /note="Bifunctional coenzyme PQQ synthesis protein C/D"
FT /id="PRO_0000219980"
FT REGION 1..267
FT /note="PqqC"
FT REGION 260..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..280
FT /note="Linker"
FT REGION 281..372
FT /note="PqqD"
FT HELIX 19..33
FT /evidence="ECO:0007829|PDB:5VRC"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:5VRC"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:5VRC"
FT HELIX 51..76
FT /evidence="ECO:0007829|PDB:5VRC"
FT HELIX 82..96
FT /evidence="ECO:0007829|PDB:5VRC"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:5VRC"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:5VRC"
FT HELIX 119..124
FT /evidence="ECO:0007829|PDB:5VRC"
FT HELIX 130..145
FT /evidence="ECO:0007829|PDB:5VRC"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:5VRC"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:5VRC"
FT HELIX 169..173
FT /evidence="ECO:0007829|PDB:5VRC"
FT HELIX 181..185
FT /evidence="ECO:0007829|PDB:5VRC"
FT HELIX 200..208
FT /evidence="ECO:0007829|PDB:5VRC"
FT HELIX 212..240
FT /evidence="ECO:0007829|PDB:5VRC"
FT TURN 253..256
FT /evidence="ECO:0007829|PDB:5VRC"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:5SXY"
FT TURN 302..305
FT /evidence="ECO:0007829|PDB:5SXY"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:5SXY"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:5SXY"
FT HELIX 320..328
FT /evidence="ECO:0007829|PDB:5SXY"
FT HELIX 335..346
FT /evidence="ECO:0007829|PDB:5SXY"
FT HELIX 350..365
FT /evidence="ECO:0007829|PDB:5SXY"
FT TURN 366..368
FT /evidence="ECO:0007829|PDB:5SXY"
SQ SEQUENCE 372 AA; 41577 MW; 3E502CEB4097695D CRC64;
MTAQFPPPVP DTEQRLLSHE ELEAALRDIG ARRYHNLHPF HRLLHDGKLS KDQVRAWALN
RYYYQAMIPV KDAALLARLP DAQLRRIWRQ RIVDHDGDHE GDGGIERWLK LAEGVGFTRD
YVLSTKGILS ATRFSVDAYV HFVSERSLLE AIASSLTEMF SPTIISERVA GMLKNYDFIT
KDTLAYFDKR LTQAPRDADF ALDYVKRHAT TPEMQRAAID ALTFKCNVLW TQLDALYFAY
VAPGMVPPDA WQPGEGLVAE TNSAEDSPAA AASPAATTAE PTAFSGSDVP RLPRGVRLRF
DEVRNKHVLL APERTFDLDD NAVAVLKLVD GRNTVSQIAQ ILGQTYDADP AIIEADILPM
LAGLAQKRVL ER
