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 27-MAY-2015, entry version 57. DE RecName: Full=Sulfite reductase MccA {ECO:0000305}; DE EC=1.8.99.1 {ECO:0000269|PubMed:22040142, ECO:0000269|PubMed:25642962}; DE Flags: Precursor; GN Name=mccA {ECO:0000269|PubMed:25642962, ECO:0000303|PubMed:22040142}; 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] {ECO:0000312|Proteomes:UP000000422} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W RC {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 RP PEPTIDE, AND 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., RA Richardson D.J., Simon J.; RT "A dedicated haem lyase is required for the maturation of a novel RT bacterial cytochrome c with unconventional covalent haem binding."; RL Mol. Microbiol. 64:1049-1060(2007). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INDUCTION BY SULFITE, RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-574; ALA-587; CYS-590 AND RP 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:0000244|PDB:4RKM, ECO:0000244|PDB:4RKN} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH HEME; HYDROGEN RP SULFITE AND COPPER IONS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL RP PROPERTIES, 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 0:0-0(2015). CC -!- FUNCTION: Respiratory sulfite reductase that catalyzes the CC reduction of sulfite to sulfide in a single step, consuming six CC electrons in the process (PubMed:22040142, PubMed:25642962). CC Required for sulfite respiration under anaerobic growth conditions CC (PubMed:22040142). Has only marginal activity with nitrite. CC {ECO:0000269|PubMed:22040142, ECO:0000269|PubMed:25642962}. CC -!- CATALYTIC ACTIVITY: H(2)S + acceptor + 3 H(2)O = SO(3)(2-) + CC reduced acceptor. {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 CC bind the copper ion. {ECO:0000269|PubMed:25642962}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000269|PubMed:17501927, CC ECO:0000269|PubMed:22040142, ECO:0000269|PubMed:25642962}; CC Note=Binds 8 heme 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 -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:17501927}. CC -!- INDUCTION: Repressed by fumarate and nitrate. Up-regulated by CC sulfite, but only in the absence of fumarate and nitrate (at CC protein level). {ECO:0000269|PubMed:22040142}. CC -!- DISRUPTION PHENOTYPE: Loss of growth based on sulfite respiration. CC {ECO:0000269|PubMed:22040142}. 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 RefSeq; NP_906626.1; NC_005090.1. DR RefSeq; WP_011138326.1; NC_005090.1. 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 ProteinModelPortal; Q7MSJ8; -. DR STRING; 273121.WS0379; -. DR EnsemblBacteria; CAE09526; CAE09526; WS0379. DR KEGG; wsu:WS0379; -. DR PATRIC; 24037854; VBIWolSuc63014_0363. DR HOGENOM; HOG000286693; -. DR OMA; EHPEVDN; -. DR OrthoDB; EOG6T4RVP; -. 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: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 Gene3D; 1.10.710.10; -; 2. DR HAMAP; MF_02023; Sulfite_red; 1. DR InterPro; IPR023155; Cyt_c-552/4. DR InterPro; IPR029467; Cytochrome_c3/c7. DR InterPro; IPR011031; Multihaem_cyt. DR Pfam; PF14522; Cytochrome_C7; 1. DR PROSITE; PS51008; MULTIHEME_CYTC; 2. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Copper; Electron transport; Heme; KW Iron; Metal-binding; Oxidoreductase; Periplasm; Reference proteome; KW Signal; Sulfate respiration; Transport. FT SIGNAL 1 39 {ECO:0000269|PubMed:17501927}. FT CHAIN 40 702 Sulfite reductase MccA. FT /FTId=PRO_0000432940. FT METAL 159 159 Iron (heme 1 axial ligand); via tele FT nitrogen. {ECO:0000244|PDB:4RKN}. FT METAL 171 171 Iron (heme 4 axial ligand); via tele FT nitrogen. {ECO:0000244|PDB:4RKN}. FT METAL 318 318 Iron (heme 2 axial ligand); via tele FT nitrogen. {ECO:0000244|PDB:4RKN}. FT METAL 355 355 Iron (heme 3 axial ligand); via tele FT nitrogen. {ECO:0000244|PDB:4RKN}. FT METAL 360 360 Iron (heme 1 axial ligand); via tele FT nitrogen. {ECO:0000244|PDB:4RKN}. FT METAL 376 376 Iron (heme 4 axial ligand); via tele FT nitrogen. {ECO:0000244|PDB:4RKN}. FT METAL 411 411 Copper. {ECO:0000269|PubMed:25642962}. FT METAL 423 423 Iron (heme 6 axial ligand); via tele FT nitrogen. {ECO:0000244|PDB:4RKN}. FT METAL 434 434 Iron (heme 5 axial ligand); via tele FT nitrogen. {ECO:0000244|PDB:4RKN}. FT METAL 437 437 Iron (heme 3 axial ligand); via tele FT nitrogen. {ECO:0000244|PDB:4RKN}. FT METAL 478 478 Iron (heme 6 axial ligand); via tele FT nitrogen. {ECO:0000244|PDB:4RKN}. FT METAL 491 491 Iron (heme 8 axial ligand); via tele FT nitrogen. {ECO:0000244|PDB:4RKN}. FT METAL 500 500 Iron (heme 7 axial ligand); via tele FT nitrogen. {ECO:0000244|PDB:4RKN}. FT METAL 507 507 Copper. {ECO:0000269|PubMed:25642962}. FT METAL 528 528 Iron (heme 5 axial ligand); via tele FT nitrogen. {ECO:0000244|PDB:4RKN}. FT METAL 591 591 Iron (heme 8 axial ligand); via tele FT nitrogen. {ECO:0000244|PDB:4RKN}. FT METAL 675 675 Iron (heme 7 axial ligand); via tele FT nitrogen. {ECO:0000244|PDB:4RKN}. FT BINDING 155 155 Heme 1 (covalent). FT {ECO:0000244|PDB:4RKN}. FT BINDING 158 158 Heme 1 (covalent). FT {ECO:0000244|PDB:4RKN}. FT BINDING 220 220 Substrate. {ECO:0000244|PDB:4RKN}. FT BINDING 297 297 Substrate. {ECO:0000244|PDB:4RKN}. FT BINDING 314 314 Heme 2 (covalent). {ECO:0000305}. FT BINDING 317 317 Heme 2 (covalent). FT {ECO:0000244|PDB:4RKN}. FT BINDING 351 351 Heme 3 (covalent). FT {ECO:0000244|PDB:4RKN}. FT BINDING 354 354 Heme 3 (covalent). FT {ECO:0000244|PDB:4RKN}. FT BINDING 372 372 Heme 4 (covalent). FT {ECO:0000244|PDB:4RKN}. FT BINDING 375 375 Heme 4 (covalent). FT {ECO:0000244|PDB:4RKN}. FT BINDING 378 378 Substrate. {ECO:0000244|PDB:4RKN}. FT BINDING 430 430 Heme 5 (covalent). FT {ECO:0000244|PDB:4RKN}. FT BINDING 433 433 Heme 5 (covalent). FT {ECO:0000244|PDB:4RKN}. FT BINDING 474 474 Heme 6 (covalent). FT {ECO:0000244|PDB:4RKN}. FT BINDING 477 477 Heme 6 (covalent). FT {ECO:0000244|PDB:4RKN}. FT BINDING 496 496 Heme 7 (covalent). FT {ECO:0000244|PDB:4RKN}. FT BINDING 499 499 Heme 7 (covalent). FT {ECO:0000244|PDB:4RKN}. FT BINDING 574 574 Heme 8 (covalent). FT {ECO:0000244|PDB:4RKN}. FT BINDING 590 590 Heme 8 (covalent). FT {ECO:0000244|PDB:4RKN}. FT MUTAGEN 574 574 C->A: Impairs protein stability and FT abolishes sulfite reductase activity; FT when associated with C-587. FT {ECO:0000269|PubMed:22040142}. FT MUTAGEN 587 587 A->C: Impairs protein stability and FT abolishes sulfite reductase activity; FT when associated with A-574. FT {ECO:0000269|PubMed:22040142}. FT MUTAGEN 587 587 A->S: No effect on protein stability and FT sulfite reductase activity. FT {ECO:0000269|PubMed:22040142}. FT MUTAGEN 590 590 C->A,S: Impairs protein stability. FT {ECO:0000269|PubMed:22040142}. FT MUTAGEN 591 591 H->A: Impairs protein stability. FT {ECO:0000269|PubMed:22040142}. 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 //