ID MCCA_WOLSU Reviewed; 702 AA. AC Q7MSJ8; DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 25-MAY-2022, entry version 88. DE RecName: Full=Dissimilatory sulfite reductase MccA {ECO:0000305}; DE EC=1.8.99.- {ECO:0000269|PubMed:22040142, ECO:0000269|PubMed:25642962}; DE Flags: Precursor; GN Name=mccA {ECO:0000303|PubMed:22040142, ECO:0000303|PubMed:25642962}; GN OrderedLocusNames=WS0379 {ECO:0000312|EMBL:CAE09526.1}; OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC OS 11488 / FDC 602W) (Vibrio succinogenes). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Wolinella. OX NCBI_TaxID=273121 {ECO:0000312|Proteomes:UP000000422}; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC RC 11488 / FDC 602W {ECO:0000312|Proteomes:UP000000422}; RX PubMed=14500908; DOI=10.1073/pnas.1932838100; RA Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O., RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B., RA Meyer F., Lederer H., Schuster S.C.; RT "Complete genome sequence and analysis of Wolinella succinogenes."; RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY, COFACTOR, SUBUNIT, SIGNAL PEPTIDE, AND RP SUBCELLULAR LOCATION. RX PubMed=17501927; DOI=10.1111/j.1365-2958.2007.05712.x; RA Hartshorne R.S., Kern M., Meyer B., Clarke T.A., Karas M., Richardson D.J., RA Simon J.; RT "A dedicated haem lyase is required for the maturation of a novel bacterial RT cytochrome c with unconventional covalent haem binding."; RL Mol. Microbiol. 64:1049-1060(2007). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INDUCTION BY SULFITE, DISRUPTION RP PHENOTYPE, AND MUTAGENESIS OF CYS-574; ALA-587; CYS-590 AND HIS-591. RX PubMed=22040142; DOI=10.1111/j.1365-2958.2011.07906.x; RA Kern M., Klotz M.G., Simon J.; RT "The Wolinella succinogenes mcc gene cluster encodes an unconventional RT respiratory sulphite reduction system."; RL Mol. Microbiol. 82:1515-1530(2011). RN [4] {ECO:0007744|PDB:4RKM, ECO:0007744|PDB:4RKN} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH HEME; HYDROGEN RP SULFITE AND COPPER IONS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, RP COFACTOR, AND SUBUNIT. RX PubMed=25642962; DOI=10.1038/nature14109; RA Hermann B., Kern M., La Pietra L., Simon J., Einsle O.; RT "The octahaem MccA is a haem c-copper sulfite reductase."; RL Nature 520:706-709(2015). 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 (PubMed:22040142, PubMed:25642962). Required for sulfite CC respiration under anaerobic growth conditions (PubMed:22040142). Has CC only marginal activity with nitrite. {ECO:0000269|PubMed:22040142, CC ECO:0000269|PubMed:25642962}. 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:22040142, CC ECO:0000269|PubMed:25642962}; CC -!- COFACTOR: CC Name=Cu(+); Xref=ChEBI:CHEBI:49552; CC Evidence={ECO:0000269|PubMed:25642962}; 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:0000269|PubMed:25642962}; CC -!- COFACTOR: CC Name=heme c; Xref=ChEBI:CHEBI:61717; CC Evidence={ECO:0000269|PubMed:17501927, ECO:0000269|PubMed:22040142, CC ECO:0000269|PubMed:25642962}; CC Note=Binds 8 heme c groups covalently per monomer. CC {ECO:0000269|PubMed:17501927, ECO:0000269|PubMed:25642962}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=44 uM for sulfite {ECO:0000269|PubMed:25642962}; CC Vmax=151 umol/min/mg enzyme with sulfite as substrate CC {ECO:0000269|PubMed:25642962}; CC -!- PATHWAY: Sulfur metabolism; sulfite reduction. {ECO:0000305}. CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:17501927, CC ECO:0000269|PubMed:25642962}. CC -!- INTERACTION: CC Q7MSJ8; Q7MSJ8: mccA; NbExp=2; IntAct=EBI-16140995, EBI-16140995; CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:17501927}. CC -!- INDUCTION: Repressed by fumarate and nitrate. Up-regulated by sulfite, CC but only in the absence of fumarate and nitrate (at protein level). CC {ECO:0000269|PubMed:22040142}. CC -!- DISRUPTION PHENOTYPE: Loss of growth based on sulfite respiration. CC {ECO:0000269|PubMed:22040142}. CC -!- MISCELLANEOUS: The eighth heme binding site has an unusual CXXXXXCH CC motif. {ECO:0000269|PubMed:25642962}. CC -!- SIMILARITY: Belongs to the multiheme cytochrome c family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX571658; CAE09526.1; -; Genomic_DNA. DR PDB; 4RKM; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=1-702. DR PDB; 4RKN; X-ray; 2.10 A; A/B/C/D=1-702. DR PDBsum; 4RKM; -. DR PDBsum; 4RKN; -. DR AlphaFoldDB; Q7MSJ8; -. DR SMR; Q7MSJ8; -. DR DIP; DIP-61512N; -. DR STRING; 273121.WS0379; -. DR EnsemblBacteria; CAE09526; CAE09526; WS0379. DR KEGG; wsu:WS0379; -. DR eggNOG; COG0484; Bacteria. DR HOGENOM; CLU_406457_0_0_7; -. DR OMA; CHPAQYE; -. DR BRENDA; 1.8.99.5; 6642. DR SABIO-RK; Q7MSJ8; -. DR UniPathway; UPA00370; -. DR Proteomes; UP000000422; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:1903136; F:cuprous ion binding; IDA:UniProtKB. DR GO; GO:0020037; F:heme binding; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0016667; F:oxidoreductase activity, acting on a sulfur group of donors; IDA:UniProtKB. DR GO; GO:0016002; F:sulfite reductase activity; IDA:UniProtKB. DR GO; GO:0009061; P:anaerobic respiration; IEA:UniProtKB-KW. DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IDA:UniProtKB. DR GO; GO:0070207; P:protein homotrimerization; IDA: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 3D-structure; Copper; Electron transport; Heme; Iron; Metal-binding; KW Oxidoreductase; Periplasm; Reference proteome; Signal; Sulfate respiration; KW Transport. FT SIGNAL 1..39 FT /evidence="ECO:0000269|PubMed:17501927" FT CHAIN 40..702 FT /note="Dissimilatory sulfite reductase MccA" FT /id="PRO_0000432940" FT METAL 159 FT /note="Iron (heme c 1 axial ligand); via tele nitrogen" FT /evidence="ECO:0007744|PDB:4RKN" FT METAL 171 FT /note="Iron (heme c 4 axial ligand); via tele nitrogen" FT /evidence="ECO:0007744|PDB:4RKN" FT METAL 318 FT /note="Iron (heme c 2 axial ligand); via tele nitrogen" FT /evidence="ECO:0007744|PDB:4RKN" FT METAL 355 FT /note="Iron (heme c 3 axial ligand); via tele nitrogen" FT /evidence="ECO:0007744|PDB:4RKN" FT METAL 360 FT /note="Iron (heme c 1 axial ligand); via tele nitrogen" FT /evidence="ECO:0007744|PDB:4RKN" FT METAL 376 FT /note="Iron (heme c 4 axial ligand); via tele nitrogen" FT /evidence="ECO:0007744|PDB:4RKN" FT METAL 411 FT /note="Cu(+)" FT /evidence="ECO:0000269|PubMed:25642962, FT ECO:0007744|PDB:4RKM" FT METAL 423 FT /note="Iron (heme c 6 axial ligand); via tele nitrogen" FT /evidence="ECO:0007744|PDB:4RKN" FT METAL 434 FT /note="Iron (heme c 5 axial ligand); via tele nitrogen" FT /evidence="ECO:0007744|PDB:4RKN" FT METAL 437 FT /note="Iron (heme c 3 axial ligand); via tele nitrogen" FT /evidence="ECO:0007744|PDB:4RKN" FT METAL 478 FT /note="Iron (heme c 6 axial ligand); via tele nitrogen" FT /evidence="ECO:0007744|PDB:4RKN" FT METAL 491 FT /note="Iron (heme c 8 axial ligand); via tele nitrogen" FT /evidence="ECO:0007744|PDB:4RKN" FT METAL 500 FT /note="Iron (heme c 7 axial ligand); via tele nitrogen" FT /evidence="ECO:0007744|PDB:4RKN" FT METAL 507 FT /note="Cu(+)" FT /evidence="ECO:0000269|PubMed:25642962, FT ECO:0007744|PDB:4RKM" FT METAL 528 FT /note="Iron (heme c 5 axial ligand); via tele nitrogen" FT /evidence="ECO:0007744|PDB:4RKN" FT METAL 591 FT /note="Iron (heme c 8 axial ligand); via tele nitrogen" FT /evidence="ECO:0007744|PDB:4RKN" FT METAL 675 FT /note="Iron (heme c 7 axial ligand); via tele nitrogen" FT /evidence="ECO:0007744|PDB:4RKN" FT BINDING 155 FT /note="Heme c 1; covalent" FT /evidence="ECO:0007744|PDB:4RKN" FT BINDING 158 FT /note="Heme c 1; covalent" FT /evidence="ECO:0007744|PDB:4RKN" FT BINDING 220 FT /note="Substrate" FT /evidence="ECO:0007744|PDB:4RKN" FT BINDING 297 FT /note="Substrate" FT /evidence="ECO:0007744|PDB:4RKN" FT BINDING 314 FT /note="Heme c 2; covalent" FT /evidence="ECO:0000305" FT BINDING 317 FT /note="Heme c 2; covalent" FT /evidence="ECO:0007744|PDB:4RKN" FT BINDING 351 FT /note="Heme c 3; covalent" FT /evidence="ECO:0007744|PDB:4RKN" FT BINDING 354 FT /note="Heme c 3; covalent" FT /evidence="ECO:0007744|PDB:4RKN" FT BINDING 372 FT /note="Heme c 4; covalent" FT /evidence="ECO:0007744|PDB:4RKN" FT BINDING 375 FT /note="Heme c 4; covalent" FT /evidence="ECO:0007744|PDB:4RKN" FT BINDING 378 FT /note="Substrate" FT /evidence="ECO:0007744|PDB:4RKN" FT BINDING 430 FT /note="Heme c 5; covalent" FT /evidence="ECO:0007744|PDB:4RKN" FT BINDING 433 FT /note="Heme c 5; covalent" FT /evidence="ECO:0007744|PDB:4RKN" FT BINDING 474 FT /note="Heme c 6; covalent" FT /evidence="ECO:0007744|PDB:4RKN" FT BINDING 477 FT /note="Heme c 6; covalent" FT /evidence="ECO:0007744|PDB:4RKN" FT BINDING 496 FT /note="Heme c 7; covalent" FT /evidence="ECO:0007744|PDB:4RKN" FT BINDING 499 FT /note="Heme c 7; covalent" FT /evidence="ECO:0007744|PDB:4RKN" FT BINDING 574 FT /note="Heme c 8; covalent" FT /evidence="ECO:0007744|PDB:4RKN" FT BINDING 590 FT /note="Heme c 8; covalent" FT /evidence="ECO:0007744|PDB:4RKN" FT MUTAGEN 574 FT /note="C->A: Impairs protein stability and abolishes FT sulfite reductase activity; when associated with C-587." FT /evidence="ECO:0000269|PubMed:22040142" FT MUTAGEN 587 FT /note="A->C: Impairs protein stability and abolishes FT sulfite reductase activity; when associated with A-574." FT /evidence="ECO:0000269|PubMed:22040142" FT MUTAGEN 587 FT /note="A->S: No effect on protein stability and sulfite FT reductase activity." FT /evidence="ECO:0000269|PubMed:22040142" FT MUTAGEN 590 FT /note="C->A,S: Impairs protein stability." FT /evidence="ECO:0000269|PubMed:22040142" FT MUTAGEN 591 FT /note="H->A: Impairs protein stability." FT /evidence="ECO:0000269|PubMed:22040142" FT HELIX 47..54 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 60..63 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 68..74 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 76..85 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 87..90 FT /evidence="ECO:0007829|PDB:4RKN" FT TURN 91..94 FT /evidence="ECO:0007829|PDB:4RKN" FT STRAND 96..102 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 105..108 FT /evidence="ECO:0007829|PDB:4RKN" FT TURN 109..111 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 112..114 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 115..121 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 124..127 FT /evidence="ECO:0007829|PDB:4RKN" FT STRAND 144..146 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 152..158 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 160..167 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 170..173 FT /evidence="ECO:0007829|PDB:4RKN" FT STRAND 174..176 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 182..184 FT /evidence="ECO:0007829|PDB:4RKN" FT STRAND 188..190 FT /evidence="ECO:0007829|PDB:4RKN" FT STRAND 192..194 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 207..209 FT /evidence="ECO:0007829|PDB:4RKN" FT STRAND 210..215 FT /evidence="ECO:0007829|PDB:4RKN" FT STRAND 219..225 FT /evidence="ECO:0007829|PDB:4RKN" FT STRAND 233..238 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 240..242 FT /evidence="ECO:0007829|PDB:4RKN" FT STRAND 245..250 FT /evidence="ECO:0007829|PDB:4RKN" FT STRAND 253..255 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 256..260 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 264..273 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 281..287 FT /evidence="ECO:0007829|PDB:4RKN" FT STRAND 297..300 FT /evidence="ECO:0007829|PDB:4RKN" FT TURN 301..303 FT /evidence="ECO:0007829|PDB:4RKN" FT STRAND 304..307 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 310..312 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 314..317 FT /evidence="ECO:0007829|PDB:4RKN" FT STRAND 320..322 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 327..333 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 337..342 FT /evidence="ECO:0007829|PDB:4RKN" FT STRAND 344..349 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 351..355 FT /evidence="ECO:0007829|PDB:4RKN" FT TURN 357..360 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 373..376 FT /evidence="ECO:0007829|PDB:4RKN" FT STRAND 379..381 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 383..387 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 390..392 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 396..399 FT /evidence="ECO:0007829|PDB:4RKN" FT STRAND 400..402 FT /evidence="ECO:0007829|PDB:4RKN" FT STRAND 408..410 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 414..419 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 422..425 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 430..433 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 459..462 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 474..477 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 479..485 FT /evidence="ECO:0007829|PDB:4RKN" FT STRAND 487..489 FT /evidence="ECO:0007829|PDB:4RKN" FT TURN 490..493 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 496..500 FT /evidence="ECO:0007829|PDB:4RKN" FT STRAND 505..508 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 511..513 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 516..518 FT /evidence="ECO:0007829|PDB:4RKN" FT STRAND 540..542 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 570..575 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 582..586 FT /evidence="ECO:0007829|PDB:4RKN" FT TURN 587..591 FT /evidence="ECO:0007829|PDB:4RKN" FT TURN 593..595 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 600..602 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 607..638 FT /evidence="ECO:0007829|PDB:4RKN" FT STRAND 642..644 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 646..669 FT /evidence="ECO:0007829|PDB:4RKN" FT TURN 672..675 FT /evidence="ECO:0007829|PDB:4RKN" FT HELIX 677..700 FT /evidence="ECO:0007829|PDB:4RKN" SQ SEQUENCE 702 AA; 78939 MW; 7F03B02298162E28 CRC64; MLSGWSVLKG GNMKYWDKAL LSLFMCVSTL SIAATHAVAM EGMQMTKEAR EIIAHPKGTK ESRGVISLQD YIVEEQAMYD WLFKNHPIFT KYGGKTVGKL VVKDRGEEWI EEGRGNDFSK ASKRSGGEGF SSMMYRVARN STLQYPNKFI GPEKCGECHP AQYETWSRSR HATTIRFPGE HPEVNNKLND PVFDKDTASI LPQGITPDVV YCTVGHIRTK FGFFDAWLLR GTYHVEGGLL KNGTGQIVAG GNQWQRTWAL NLSPEVAKKI KKWVPDFPVT LEEYGDNGGY VRGLASYAAK YKKSMSFQAS TSYCEVCHPW KFDFKNESEF YAALGNAKEL QKHTISKGVS CEECHGAGGH LEGGSGLLIS NCERCHQRFS YSPDLMRNNP LNAGKPDLAL SSKFKSMGPG CGSEGSQTYF TAHYEKGMRC ATCHDPHDVT GNVTGEKGIK GVSYNSEQGY LSSLYSKPKL KKECTDCHKE QAYIQSKADT HSKNSCASCH MPFMMSCENF YAIQFQDQAG FDTQRRAHIW KIDVDPARKS LVAGSTSKDP RDGKDWHFER NEEGRNFVDL MWACARTTWA DKDQAEAKGC HSPVVSELKE TLHFKDQKQV YNEVMGWQTP VKDKFTQVKV GIQGLYSLLE VKKLAPSDKT RVYELIEKAQ DTVDLIEKDG SWGMHGFKYT KQRLDAAVEY INEAQRIMKK SL //