MCCA_SHEON
ID MCCA_SHEON Reviewed; 708 AA.
AC Q8EJI6;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Dissimilatory sulfite reductase SirA {ECO:0000305};
DE EC=1.8.99.- {ECO:0000269|PubMed:21199252};
DE Flags: Precursor;
GN Name=sirA {ECO:0000303|PubMed:21199252, ECO:0000312|EMBL:AAN53560.2};
GN Synonyms=mccA {ECO:0000303|PubMed:21199252};
GN OrderedLocusNames=SO_0479 {ECO:0000312|EMBL:AAN53560.2};
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586 {ECO:0000312|EMBL:AAN53560.2};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1 {ECO:0000312|EMBL:AAN53560.2};
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=MR-1 {ECO:0000303|PubMed:21199252};
RX PubMed=21199252; DOI=10.1111/j.1462-2920.2010.02313.x;
RA Shirodkar S., Reed S., Romine M., Saffarini D.;
RT "The octahaem SirA catalyses dissimilatory sulfite reduction in Shewanella
RT oneidensis MR-1.";
RL Environ. Microbiol. 13:108-115(2011).
CC -!- FUNCTION: Respiratory sulfite reductase that catalyzes the reduction of
CC sulfite to sulfide in a single step, consuming six electrons in the
CC process. Required for sulfite respiration under anaerobic growth
CC conditions. Does not contribute to nitrite reduction.
CC {ECO:0000269|PubMed:21199252}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-disulfide + 2 A + 3 H2O + hydrogen sulfide =
CC [protein]-dithiol + 2 AH2 + H(+) + sulfite; Xref=Rhea:RHEA:51676,
CC Rhea:RHEA-COMP:10593, Rhea:RHEA-COMP:10594, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:29919, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:50058; Evidence={ECO:0000269|PubMed:21199252};
CC -!- COFACTOR:
CC Name=Cu(+); Xref=ChEBI:CHEBI:49552;
CC Evidence={ECO:0000250|UniProtKB:Q7MSJ8};
CC Note=Exposure to oxygen reduces copper binding and leads to the
CC formation of a disulfide bond between the two Cys residues that bind
CC the copper ion. {ECO:0000250|UniProtKB:Q7MSJ8};
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000250|UniProtKB:Q7MSJ8};
CC Note=Binds 8 heme c groups covalently per monomer.
CC {ECO:0000250|UniProtKB:Q7MSJ8};
CC -!- PATHWAY: Sulfur metabolism; sulfite reduction. {ECO:0000305}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q7MSJ8}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:Q7MSJ8}.
CC -!- DISRUPTION PHENOTYPE: Loss of growth based on sulfite respiration.
CC {ECO:0000269|PubMed:21199252}.
CC -!- MISCELLANEOUS: The eighth heme binding site has an unusual CXXXXXCH
CC motif. {ECO:0000250|UniProtKB:Q7MSJ8}.
CC -!- SIMILARITY: Belongs to the multiheme cytochrome c family.
CC {ECO:0000305}.
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DR EMBL; AE014299; AAN53560.2; -; Genomic_DNA.
DR RefSeq; NP_716115.2; NC_004347.2.
DR RefSeq; WP_011070829.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EJI6; -.
DR SMR; Q8EJI6; -.
DR STRING; 211586.SO_0479; -.
DR PaxDb; Q8EJI6; -.
DR KEGG; son:SO_0479; -.
DR PATRIC; fig|211586.12.peg.464; -.
DR eggNOG; COG0484; Bacteria.
DR HOGENOM; CLU_406457_0_0_6; -.
DR OMA; CHPAQYE; -.
DR OrthoDB; 738283at2; -.
DR BioCyc; MetaCyc:MON-20180; -.
DR BioCyc; SONE211586:G1GMP-455-MON; -.
DR UniPathway; UPA00370; -.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:1903136; F:cuprous ion binding; ISS:UniProtKB.
DR GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016667; F:oxidoreductase activity, acting on a sulfur group of donors; IMP:UniProtKB.
DR GO; GO:0016002; F:sulfite reductase activity; IMP:UniProtKB.
DR GO; GO:0009061; P:anaerobic respiration; IEA:UniProtKB-KW.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IMP:UniProtKB.
DR HAMAP; MF_02023; Sulfite_red; 1.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR InterPro; IPR032897; Sulfite_reductase.
DR SUPFAM; SSF48695; SSF48695; 1.
DR PROSITE; PS51008; MULTIHEME_CYTC; 2.
PE 1: Evidence at protein level;
KW Copper; Electron transport; Heme; Iron; Metal-binding; Oxidoreductase;
KW Periplasm; Reference proteome; Signal; Sulfate respiration; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..708
FT /note="Dissimilatory sulfite reductase SirA"
FT /id="PRO_0000432941"
FT BINDING 173
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 176
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 177
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
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 BINDING 189
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 332
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 335
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 336
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 369
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 372
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 373
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
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 BINDING 378
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
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 BINDING 391
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 394
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 395
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 397
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 429
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 441
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
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 BINDING 448
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 451
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 452
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 455
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
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 BINDING 475
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="6"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 478
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="6"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 479
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
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 BINDING 492
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="8"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 497
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="7"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 500
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="7"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 501
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="7"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 508
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 529
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 575
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="8"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 591
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="8"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 592
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="8"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
FT BINDING 676
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="7"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q7MSJ8"
SQ SEQUENCE 708 AA; 79125 MW; 73A059BA4FDCBF69 CRC64;
MKRWKTKTAL GVLFCLGSAV SATTIASDAK SDGKVVPGVG NKQQTHYTQD ILANPKVSEN
LMEKSRGVKT LQDYIVQEQE LFDFLFENHP VFKYDAEGRL KGTYKVSDRG EEYLHGGDSV
AYSKHSKEVN STDGTAVRYS AYEDGQRPKA LQYRLGAKSI LDFPNKFVGP EKCGECHGPQ
YEKWRRSRHS KTIRFPGEHP EVDNDLKKPM YTTKDTSILP SGITPDAIYA TVGTPRTKYG
FIDAYLVRGT YHVKDGLLKD GTGTMVAGGN QFSRGWAEWL TPEMAAKINK AIPSFPLKME
DFGTSGSHQW GMSSYGAKYE KEFLFQPASS YCEMCHSFKF DFQTKEEFFA ALGNPKELQK
HTISKGITCE ECHGAGGHLD GGIGGGMPSN CERCHQRFNF VEELAETPQG QEKLEYAFNV
KMKSSCPSCG TEGSQMFASA HYDKGMRCST CHDPHEVTDG DWKSGITKPK IIKECTDCHT
AQAEIAKNTN THSNQTCQSC HMPNMGSCEN FTAIQFPDMA GFDNVRKSHM WKIDVDPLRK
TLNPPEGKSR DATTKGWTVA KDENGYNYLD LMWTCARTSA SDHDVTENKG CHSQFQSELE
VGLHFEDQME IYGEVQKWQK PVKDLFGQVL QGLQRIDKLL EVTQLPVDKK TEVLMLTDKA
QDVIKLVEAD GSWGAHGPRY TQKRLDAALT YVQQAQAIID GNGYNAKM
