QRCA_DESVH
ID QRCA_DESVH Reviewed; 210 AA.
AC P0DOV3;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Menaquinone reductase, multiheme cytochrome c subunit {ECO:0000305|PubMed:20498375};
DE EC=1.97.-.-;
DE AltName: Full=Quinone reductase complex subunit A {ECO:0000303|PubMed:20498375};
DE AltName: Full=Type I cytochrome c3:menaquinone oxidoreductase subunit A {ECO:0000303|PubMed:20498375};
GN Name=qrcA {ECO:0000303|PubMed:20498375};
GN OrderedLocusNames=DVU_0695.1 {ECO:0000305};
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA Wall J.D., Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
RN [2]
RP PROTEIN SEQUENCE OF 1-5, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=20498375; DOI=10.1074/jbc.m110.124305;
RA Venceslau S.S., Lino R.R., Pereira I.A.;
RT "The Qrc membrane complex, related to the alternative complex III, is a
RT menaquinone reductase involved in sulfate respiration.";
RL J. Biol. Chem. 285:22774-22783(2010).
RN [3]
RP INTERACTION WITH [NIFE] HYDROGENASE AND TPIC(3), AND COFACTOR.
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=21651911; DOI=10.1016/j.febslet.2011.05.054;
RA Venceslau S.S., Matos D., Pereira I.A.;
RT "EPR characterization of the new Qrc complex from sulfate reducing bacteria
RT and its ability to form a supercomplex with hydrogenase and TpIc3.";
RL FEBS Lett. 585:2177-2181(2011).
CC -!- FUNCTION: Component of the respiratory Qrc complex, that catalyzes the
CC reduction of the menaquinone pool using electrons transferred from the
CC reduced periplasmic cytochrome c3, and which is probably involved in
CC sulfate respiration. Is likely essential for growth on H(2) or formate
CC since the periplasmic hydrogenases and/or formate dehydrogenases act as
CC primary electron donors for the Qrc complex.
CC {ECO:0000269|PubMed:20498375}.
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000269|PubMed:20498375, ECO:0000269|PubMed:21651911};
CC Note=Binds 6 heme c groups covalently per subunit.
CC {ECO:0000269|PubMed:20498375};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.8 uM for the cytochrome c3 {ECO:0000269|PubMed:20498375};
CC KM=4.0 uM for menaquinone-4 {ECO:0000269|PubMed:20498375};
CC Vmax=92 nmol/min/mg enzyme {ECO:0000269|PubMed:20498375};
CC Note=kcat is 16.6 min(-1). Values are measured with the whole Qrc
CC complex. {ECO:0000269|PubMed:20498375};
CC -!- SUBUNIT: The Qrc complex is composed of four subunits: QrcA, QrcB, QrcC
CC and QrcD (PubMed:20498375). Can form a supercomplex with the [NiFe]
CC hydrogenase HynA1 and the tetraheme Type I cytochrome c3 TpIc(3), its
CC physiological electron donors (PubMed:21651911).
CC {ECO:0000269|PubMed:20498375, ECO:0000269|PubMed:21651911}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:20498375}; Single-pass membrane protein
CC {ECO:0000255, ECO:0000305|PubMed:20498375}; Periplasmic side
CC {ECO:0000305|PubMed:20498375}.
CC -!- SIMILARITY: Belongs to the multiheme cytochrome c family.
CC {ECO:0000305}.
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DR EMBL; AE017285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; WP_010940677.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_003858606.1; NC_002937.3.
DR AlphaFoldDB; P0DOV3; -.
DR Proteomes; UP000002194; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009061; P:anaerobic respiration; IEA:UniProtKB-KW.
DR InterPro; IPR020942; Cyt_c_III_dom.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR InterPro; IPR039118; QrcA.
DR PANTHER; PTHR39425; PTHR39425; 1.
DR Pfam; PF02085; Cytochrom_CIII; 1.
DR SUPFAM; SSF48695; SSF48695; 1.
DR PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Direct protein sequencing;
KW Electron transport; Heme; Iron; Membrane; Metal-binding; Oxidoreductase;
KW Reference proteome; Sulfate respiration; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..210
FT /note="Menaquinone reductase, multiheme cytochrome c
FT subunit"
FT /id="PRO_0000437998"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 67
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8,
FT ECO:0000305|PubMed:20498375"
FT BINDING 70
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8,
FT ECO:0000305|PubMed:20498375"
FT BINDING 71
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8,
FT ECO:0000305|PubMed:20498375"
FT BINDING 88
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000305|PubMed:20498375"
FT BINDING 91
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000305|PubMed:20498375"
FT BINDING 92
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305|PubMed:20498375"
FT BINDING 140
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8,
FT ECO:0000305|PubMed:20498375"
FT BINDING 143
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8,
FT ECO:0000305|PubMed:20498375"
FT BINDING 144
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8,
FT ECO:0000305|PubMed:20498375"
FT BINDING 152
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000305|PubMed:20498375"
FT BINDING 155
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000305|PubMed:20498375"
FT BINDING 156
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305|PubMed:20498375"
FT BINDING 186
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8,
FT ECO:0000305|PubMed:20498375"
FT BINDING 189
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000305|PubMed:20498375"
FT BINDING 190
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305|PubMed:20498375"
FT BINDING 205
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="6"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8,
FT ECO:0000305|PubMed:20498375"
FT BINDING 208
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="6"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8,
FT ECO:0000305|PubMed:20498375"
FT BINDING 209
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="6"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8,
FT ECO:0000305|PubMed:20498375"
SQ SEQUENCE 210 AA; 23605 MW; 31C1316ACC4E7D58 CRC64;
MEDRQLTNAD NENGRKCACG GAAPFFVGLV VALVFGWWAF PEMLYSQKEQ PIRFSHKVHV
NDAGMECKQC HSLREDGSFA GLPSTASCAE CHSDVLGSDP EEARFVAEYV KSGKEVKWLV
YQYQPDNVFF SHAAHSLDGC NQCHQFSERE LCNLCHLDVA DSDKAPTHYE NKLTGYSKQT
MKMWQCERCH ANENHLGVTN SSNACFVCHK
