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 02-NOV-2016, entry version 67. 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 / 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 520:706-709(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: Hydrogen sulfide + a [protein]-disulfide + 2 CC acceptor + 3 H(2)O = sulfite + a [protein]-dithiol + 2 reduced CC acceptor + 2 H(+). {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 -!- MISCELLANEOUS: The eighth heme binding site has an unusual CC CXXXXXCH 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 ProteinModelPortal; Q7MSJ8; -. DR SMR; Q7MSJ8; -. DR DIP; DIP-61512N; -. DR STRING; 273121.WS0379; -. DR EnsemblBacteria; CAE09526; CAE09526; WS0379. DR KEGG; wsu:WS0379; -. DR PATRIC; 24037854; VBIWolSuc63014_0363. DR eggNOG; ENOG4105V2T; Bacteria. DR eggNOG; ENOG410XSMT; LUCA. DR HOGENOM; HOG000286693; -. DR OMA; EHPEVDN; -. DR OrthoDB; POG091H0S4L; -. 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:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. 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; IPR011031; Multihaem_cyt. DR InterPro; IPR032897; Sulfite_reductase. DR SUPFAM; SSF48695; SSF48695; 3. 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 Dissimilatory 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); atypical. FT {ECO:0000244|PDB:4RKN}. FT BINDING 590 590 Heme 8 (covalent); atypical. 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}. FT HELIX 47 54 {ECO:0000244|PDB:4RKN}. FT HELIX 60 63 {ECO:0000244|PDB:4RKN}. FT HELIX 68 74 {ECO:0000244|PDB:4RKN}. FT HELIX 76 85 {ECO:0000244|PDB:4RKN}. FT HELIX 87 90 {ECO:0000244|PDB:4RKN}. FT TURN 91 94 {ECO:0000244|PDB:4RKN}. FT STRAND 96 102 {ECO:0000244|PDB:4RKN}. FT HELIX 105 108 {ECO:0000244|PDB:4RKN}. FT TURN 109 111 {ECO:0000244|PDB:4RKN}. FT HELIX 112 114 {ECO:0000244|PDB:4RKN}. FT HELIX 115 121 {ECO:0000244|PDB:4RKN}. FT HELIX 124 127 {ECO:0000244|PDB:4RKN}. FT STRAND 144 146 {ECO:0000244|PDB:4RKN}. FT HELIX 152 158 {ECO:0000244|PDB:4RKN}. FT HELIX 160 167 {ECO:0000244|PDB:4RKN}. FT HELIX 170 173 {ECO:0000244|PDB:4RKN}. FT STRAND 174 176 {ECO:0000244|PDB:4RKN}. FT HELIX 182 184 {ECO:0000244|PDB:4RKN}. FT STRAND 188 190 {ECO:0000244|PDB:4RKN}. FT STRAND 192 194 {ECO:0000244|PDB:4RKN}. FT HELIX 207 209 {ECO:0000244|PDB:4RKN}. FT STRAND 210 215 {ECO:0000244|PDB:4RKN}. FT STRAND 219 225 {ECO:0000244|PDB:4RKN}. FT STRAND 233 238 {ECO:0000244|PDB:4RKN}. FT HELIX 240 242 {ECO:0000244|PDB:4RKN}. FT STRAND 245 250 {ECO:0000244|PDB:4RKN}. FT STRAND 253 255 {ECO:0000244|PDB:4RKN}. FT HELIX 256 260 {ECO:0000244|PDB:4RKN}. FT HELIX 264 273 {ECO:0000244|PDB:4RKN}. FT HELIX 281 287 {ECO:0000244|PDB:4RKN}. FT STRAND 297 300 {ECO:0000244|PDB:4RKN}. FT TURN 301 303 {ECO:0000244|PDB:4RKN}. FT STRAND 304 307 {ECO:0000244|PDB:4RKN}. FT HELIX 310 312 {ECO:0000244|PDB:4RKN}. FT HELIX 314 317 {ECO:0000244|PDB:4RKN}. FT STRAND 320 322 {ECO:0000244|PDB:4RKN}. FT HELIX 327 333 {ECO:0000244|PDB:4RKN}. FT HELIX 337 342 {ECO:0000244|PDB:4RKN}. FT STRAND 344 349 {ECO:0000244|PDB:4RKN}. FT HELIX 351 355 {ECO:0000244|PDB:4RKN}. FT TURN 357 360 {ECO:0000244|PDB:4RKN}. FT HELIX 373 376 {ECO:0000244|PDB:4RKN}. FT STRAND 379 381 {ECO:0000244|PDB:4RKN}. FT HELIX 383 387 {ECO:0000244|PDB:4RKN}. FT HELIX 390 392 {ECO:0000244|PDB:4RKN}. FT HELIX 396 399 {ECO:0000244|PDB:4RKN}. FT STRAND 400 402 {ECO:0000244|PDB:4RKN}. FT STRAND 408 410 {ECO:0000244|PDB:4RKN}. FT HELIX 414 419 {ECO:0000244|PDB:4RKN}. FT HELIX 422 425 {ECO:0000244|PDB:4RKN}. FT HELIX 430 433 {ECO:0000244|PDB:4RKN}. FT HELIX 459 462 {ECO:0000244|PDB:4RKN}. FT HELIX 474 477 {ECO:0000244|PDB:4RKN}. FT HELIX 479 485 {ECO:0000244|PDB:4RKN}. FT STRAND 487 489 {ECO:0000244|PDB:4RKN}. FT TURN 490 493 {ECO:0000244|PDB:4RKN}. FT HELIX 496 500 {ECO:0000244|PDB:4RKN}. FT STRAND 505 508 {ECO:0000244|PDB:4RKN}. FT HELIX 511 513 {ECO:0000244|PDB:4RKN}. FT HELIX 516 518 {ECO:0000244|PDB:4RKN}. FT STRAND 540 542 {ECO:0000244|PDB:4RKN}. FT HELIX 570 575 {ECO:0000244|PDB:4RKN}. FT HELIX 582 586 {ECO:0000244|PDB:4RKN}. FT TURN 587 591 {ECO:0000244|PDB:4RKN}. FT TURN 593 595 {ECO:0000244|PDB:4RKN}. FT HELIX 600 602 {ECO:0000244|PDB:4RKN}. FT HELIX 607 638 {ECO:0000244|PDB:4RKN}. FT STRAND 642 644 {ECO:0000244|PDB:4RKN}. FT HELIX 646 669 {ECO:0000244|PDB:4RKN}. FT TURN 672 675 {ECO:0000244|PDB:4RKN}. FT HELIX 677 700 {ECO:0000244|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 //