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Database: UniProt
Entry: Q72E85
LinkDB: Q72E85
Original site: Q72E85 
ID   QRCC_DESVH              Reviewed;         255 AA.
AC   Q72E85;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   10-APR-2019, entry version 98.
DE   RecName: Full=Menaquinone reductase, iron-sulfur cluster-binding subunit {ECO:0000305|PubMed:20498375};
DE            EC=1.97.-.-;
DE   AltName: Full=Quinone reductase complex subunit C {ECO:0000303|PubMed:20498375};
DE   AltName: Full=Type I cytochrome c3:menaquinone oxidoreductase subunit C {ECO:0000303|PubMed:20498375};
GN   Name=qrcC {ECO:0000303|PubMed:20498375};
GN   OrderedLocusNames=DVU_0693 {ECO:0000312|EMBL:AAS95174.1};
OS   Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 /
OS   NCIMB 8303).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303;
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.,
RA   Dimitrov G., Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R.,
RA   Feldblyum T.V., 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 2-7, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303;
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
RT   a 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=Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303;
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
RT   bacteria and its ability to form a supercomplex with hydrogenase and
RT   TpIc3.";
RL   FEBS Lett. 585:2177-2181(2011).
CC   -!- FUNCTION: Component of the respiratory Qrc complex, that catalyzes
CC       the reduction of the menaquinone pool using electrons transferred
CC       from the reduced periplasmic cytochrome c3, and which is probably
CC       involved in sulfate respiration. Is likely essential for growth on
CC       H(2) or formate since the periplasmic hydrogenases and/or formate
CC       dehydrogenases act as primary electron donors for the Qrc complex.
CC       QrcC is an electron-transferring subunit; its cubane iron sulfur
CC       clusters form a pathway for electron transfer between the hemes of
CC       QrcA and the membrane quinone pool. {ECO:0000269|PubMed:20498375}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000269|PubMed:20498375,
CC         ECO:0000269|PubMed:21651911};
CC       Note=Binds 3 [4Fe-4S] cluster per subunit.
CC       {ECO:0000269|PubMed:20498375, ECO:0000269|PubMed:21651911};
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000269|PubMed:20498375,
CC         ECO:0000269|PubMed:21651911};
CC       Note=Binds 1 [3Fe-4S] cluster per subunit.
CC       {ECO:0000269|PubMed:20498375, ECO:0000269|PubMed:21651911};
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
CC         Qrc complex. {ECO:0000269|PubMed:20498375};
CC   -!- SUBUNIT: The Qrc complex is composed of four subunits: QrcA, QrcB,
CC       QrcC and QrcD (PubMed:20498375). Can form a supercomplex with the
CC       [NiFe] hydrogenase HynA1 and the tetraheme Type I cytochrome c3
CC       TpIc(3), its physiological electron donors (PubMed:21651911).
CC       {ECO:0000269|PubMed:20498375, ECO:0000269|PubMed:21651911}.
CC   -!- INTERACTION:
CC       Q72E84:qrcB; NbExp=2; IntAct=EBI-10070807, EBI-6974672;
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:20498375}.
DR   EMBL; AE017285; AAS95174.1; -; Genomic_DNA.
DR   RefSeq; WP_010937996.1; NC_002937.3.
DR   RefSeq; YP_009915.1; NC_002937.3.
DR   ProteinModelPortal; Q72E85; -.
DR   IntAct; Q72E85; 1.
DR   STRING; 882.DVU_0693; -.
DR   PaxDb; Q72E85; -.
DR   EnsemblBacteria; AAS95174; AAS95174; DVU_0693.
DR   GeneID; 2793633; -.
DR   KEGG; dvu:DVU0693; -.
DR   PATRIC; fig|882.5.peg.649; -.
DR   eggNOG; ENOG4107SFQ; Bacteria.
DR   eggNOG; COG0437; LUCA.
DR   KO; K00184; -.
DR   OMA; MRPVFVI; -.
DR   PhylomeDB; Q72E85; -.
DR   BioCyc; DVUL882:G1GT1-719-MONOMER; -.
DR   Proteomes; UP000002194; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009061; P:anaerobic respiration; IEA:UniProtKB-KW.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   Pfam; PF00037; Fer4; 1.
DR   Pfam; PF13247; Fer4_11; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 3.
PE   1: Evidence at protein level;
KW   3Fe-4S; 4Fe-4S; Complete proteome; Direct protein sequencing;
KW   Electron transport; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW   Periplasm; Reference proteome; Sulfate respiration; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:20498375}.
FT   CHAIN         2    255       Menaquinone reductase, iron-sulfur
FT                                cluster-binding subunit.
FT                                /FTId=PRO_0000438000.
FT   DOMAIN       11     41       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       66     97       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       99    128       4Fe-4S ferredoxin-type 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        20     20       Iron-sulfur (4Fe-4S) 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        23     23       Iron-sulfur (4Fe-4S) 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        26     26       Iron-sulfur (4Fe-4S) 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        30     30       Iron-sulfur (4Fe-4S) 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        75     75       Iron-sulfur (4Fe-4S) 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        78     78       Iron-sulfur (4Fe-4S) 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        83     83       Iron-sulfur (4Fe-4S) 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        87     87       Iron-sulfur (4Fe-4S) 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       108    108       Iron-sulfur (4Fe-4S) 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       111    111       Iron-sulfur (4Fe-4S) 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       114    114       Iron-sulfur (4Fe-4S) 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       118    118       Iron-sulfur (4Fe-4S) 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       155    155       Iron-sulfur (3Fe-4S). {ECO:0000305}.
FT   METAL       158    158       Iron-sulfur (3Fe-4S). {ECO:0000305}.
FT   METAL       188    188       Iron-sulfur (3Fe-4S). {ECO:0000305}.
FT   METAL       192    192       Iron-sulfur (3Fe-4S). {ECO:0000305}.
SQ   SEQUENCE   255 AA;  29043 MW;  4FE7CC9F3CA5C426 CRC64;
     MSSFKEFKIK WGMVIDLDKC TGCGACMVAC QAENNIAPQP DASNKLKSLN WLVVYELNNG
     KPFPEHDVAY LPRPCMQCGK PSCVSVCPVV ATDKNEEGGI VSQVYPRCIG CRYCMASCPY
     HARYFNWFDP TWPEGMDKTL TPDVSVRPRG VVEKCTFCHH RFMQAKDKAR VEGRDPSALR
     DGDYVTSCTE ACPNGAIIFG DFNNPEHRVH ELHKSKYAFR LLERLGTDPQ VYYLSRREWV
     RRLGDNYLEH EKVKG
//
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