Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dissimilatory sulfite reductase MccA

Gene

mccA

Organism
Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W) (Vibrio succinogenes)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Respiratory sulfite reductase that catalyzes the reduction of sulfite to sulfide in a single step, consuming six electrons in the process (PubMed:22040142, PubMed:25642962). Required for sulfite respiration under anaerobic growth conditions (PubMed:22040142). Has only marginal activity with nitrite.2 Publications

Miscellaneous

The eighth heme binding site has an unusual CXXXXXCH motif.1 Publication

Catalytic activityi

Hydrogen sulfide + a [protein]-disulfide + 2 acceptor + 3 H2O = sulfite + a [protein]-dithiol + 2 reduced acceptor + 2 H+.2 Publications

Cofactori

Protein has several cofactor binding sites:

Kineticsi

  1. KM=44 µM for sulfite1 Publication
  1. Vmax=151 µmol/min/mg enzyme with sulfite as substrate1 Publication

Pathwayi: sulfite reduction

This protein is involved in the pathway sulfite reduction, which is part of Sulfur metabolism.Curated
View all proteins of this organism that are known to be involved in the pathway sulfite reduction and in Sulfur metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei155Heme 1 (covalent)Combined sources1
Binding sitei158Heme 1 (covalent)Combined sources1
Metal bindingi159Iron (heme 1 axial ligand); via tele nitrogenCombined sources1
Metal bindingi171Iron (heme 4 axial ligand); via tele nitrogenCombined sources1
Binding sitei220SubstrateCombined sources1
Binding sitei297SubstrateCombined sources1
Binding sitei314Heme 2 (covalent)Curated1
Binding sitei317Heme 2 (covalent)Combined sources1
Metal bindingi318Iron (heme 2 axial ligand); via tele nitrogenCombined sources1
Binding sitei351Heme 3 (covalent)Combined sources1
Binding sitei354Heme 3 (covalent)Combined sources1
Metal bindingi355Iron (heme 3 axial ligand); via tele nitrogenCombined sources1
Metal bindingi360Iron (heme 1 axial ligand); via tele nitrogenCombined sources1
Binding sitei372Heme 4 (covalent)Combined sources1
Binding sitei375Heme 4 (covalent)Combined sources1
Metal bindingi376Iron (heme 4 axial ligand); via tele nitrogenCombined sources1
Binding sitei378SubstrateCombined sources1
Metal bindingi411Copper1 Publication1
Metal bindingi423Iron (heme 6 axial ligand); via tele nitrogenCombined sources1
Binding sitei430Heme 5 (covalent)Combined sources1
Binding sitei433Heme 5 (covalent)Combined sources1
Metal bindingi434Iron (heme 5 axial ligand); via tele nitrogenCombined sources1
Metal bindingi437Iron (heme 3 axial ligand); via tele nitrogenCombined sources1
Binding sitei474Heme 6 (covalent)Combined sources1
Binding sitei477Heme 6 (covalent)Combined sources1
Metal bindingi478Iron (heme 6 axial ligand); via tele nitrogenCombined sources1
Metal bindingi491Iron (heme 8 axial ligand); via tele nitrogenCombined sources1
Binding sitei496Heme 7 (covalent)Combined sources1
Binding sitei499Heme 7 (covalent)Combined sources1
Metal bindingi500Iron (heme 7 axial ligand); via tele nitrogenCombined sources1
Metal bindingi507Copper1 Publication1
Metal bindingi528Iron (heme 5 axial ligand); via tele nitrogenCombined sources1
Binding sitei574Heme 8 (covalent); atypicalCombined sources1
Binding sitei590Heme 8 (covalent); atypicalCombined sources1
Metal bindingi591Iron (heme 8 axial ligand); via tele nitrogenCombined sources1
Metal bindingi675Iron (heme 7 axial ligand); via tele nitrogenCombined sources1

GO - Molecular functioni

  • cuprous ion binding Source: UniProtKB
  • heme binding Source: UniProtKB
  • oxidoreductase activity, acting on a sulfur group of donors Source: UniProtKB
  • sulfite reductase activity Source: UniProtKB

GO - Biological processi

  • anaerobic respiration Source: UniProtKB-KW
  • hydrogen sulfide biosynthetic process Source: UniProtKB
  • protein homotrimerization Source: UniProtKB

Keywordsi

Molecular functionOxidoreductase
Biological processElectron transport, Sulfate respiration, Transport
LigandCopper, Heme, Iron, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00370.

Names & Taxonomyi

Protein namesi
Recommended name:
Dissimilatory sulfite reductase MccACurated (EC:1.8.99.-2 Publications)
Gene namesi
Name:mccA2 Publications
Ordered Locus Names:WS0379Imported
OrganismiWolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W) (Vibrio succinogenes)Imported
Taxonomic identifieri273121 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeWolinella
Proteomesi
  • UP000000422 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Disruption phenotypei

Loss of growth based on sulfite respiration.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi574C → A: Impairs protein stability and abolishes sulfite reductase activity; when associated with C-587. 1 Publication1
Mutagenesisi587A → C: Impairs protein stability and abolishes sulfite reductase activity; when associated with A-574. 1 Publication1
Mutagenesisi587A → S: No effect on protein stability and sulfite reductase activity. 1 Publication1
Mutagenesisi590C → A or S: Impairs protein stability. 1 Publication1
Mutagenesisi591H → A: Impairs protein stability. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 391 PublicationAdd BLAST39
ChainiPRO_000043294040 – 702Dissimilatory sulfite reductase MccAAdd BLAST663

Expressioni

Inductioni

Repressed by fumarate and nitrate. Up-regulated by sulfite, but only in the absence of fumarate and nitrate (at protein level).1 Publication

Interactioni

Subunit structurei

Homotrimer.2 Publications

Protein-protein interaction databases

DIPiDIP-61512N.
STRINGi273121.WS0379.

Structurei

Secondary structure

1702
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi47 – 54Combined sources8
Helixi60 – 63Combined sources4
Helixi68 – 74Combined sources7
Helixi76 – 85Combined sources10
Helixi87 – 90Combined sources4
Turni91 – 94Combined sources4
Beta strandi96 – 102Combined sources7
Helixi105 – 108Combined sources4
Turni109 – 111Combined sources3
Helixi112 – 114Combined sources3
Helixi115 – 121Combined sources7
Helixi124 – 127Combined sources4
Beta strandi144 – 146Combined sources3
Helixi152 – 158Combined sources7
Helixi160 – 167Combined sources8
Helixi170 – 173Combined sources4
Beta strandi174 – 176Combined sources3
Helixi182 – 184Combined sources3
Beta strandi188 – 190Combined sources3
Beta strandi192 – 194Combined sources3
Helixi207 – 209Combined sources3
Beta strandi210 – 215Combined sources6
Beta strandi219 – 225Combined sources7
Beta strandi233 – 238Combined sources6
Helixi240 – 242Combined sources3
Beta strandi245 – 250Combined sources6
Beta strandi253 – 255Combined sources3
Helixi256 – 260Combined sources5
Helixi264 – 273Combined sources10
Helixi281 – 287Combined sources7
Beta strandi297 – 300Combined sources4
Turni301 – 303Combined sources3
Beta strandi304 – 307Combined sources4
Helixi310 – 312Combined sources3
Helixi314 – 317Combined sources4
Beta strandi320 – 322Combined sources3
Helixi327 – 333Combined sources7
Helixi337 – 342Combined sources6
Beta strandi344 – 349Combined sources6
Helixi351 – 355Combined sources5
Turni357 – 360Combined sources4
Helixi373 – 376Combined sources4
Beta strandi379 – 381Combined sources3
Helixi383 – 387Combined sources5
Helixi390 – 392Combined sources3
Helixi396 – 399Combined sources4
Beta strandi400 – 402Combined sources3
Beta strandi408 – 410Combined sources3
Helixi414 – 419Combined sources6
Helixi422 – 425Combined sources4
Helixi430 – 433Combined sources4
Helixi459 – 462Combined sources4
Helixi474 – 477Combined sources4
Helixi479 – 485Combined sources7
Beta strandi487 – 489Combined sources3
Turni490 – 493Combined sources4
Helixi496 – 500Combined sources5
Beta strandi505 – 508Combined sources4
Helixi511 – 513Combined sources3
Helixi516 – 518Combined sources3
Beta strandi540 – 542Combined sources3
Helixi570 – 575Combined sources6
Helixi582 – 586Combined sources5
Turni587 – 591Combined sources5
Turni593 – 595Combined sources3
Helixi600 – 602Combined sources3
Helixi607 – 638Combined sources32
Beta strandi642 – 644Combined sources3
Helixi646 – 669Combined sources24
Turni672 – 675Combined sources4
Helixi677 – 700Combined sources24

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4RKMX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L1-702[»]
4RKNX-ray2.10A/B/C/D1-702[»]
ProteinModelPortaliQ7MSJ8.
SMRiQ7MSJ8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the multiheme cytochrome c family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105V2T. Bacteria.
ENOG410XSMT. LUCA.
HOGENOMiHOG000286693.
OMAiEHPEVDN.
OrthoDBiPOG091H0S4L.

Family and domain databases

HAMAPiMF_02023. Sulfite_red. 1 hit.
InterProiView protein in InterPro
IPR011031. Multihaem_cyt.
IPR032897. Sulfite_reductase.
SUPFAMiSSF48695. SSF48695. 3 hits.
PROSITEiView protein in PROSITE
PS51008. MULTIHEME_CYTC. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q7MSJ8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSGWSVLKG GNMKYWDKAL LSLFMCVSTL SIAATHAVAM EGMQMTKEAR
60 70 80 90 100
EIIAHPKGTK ESRGVISLQD YIVEEQAMYD WLFKNHPIFT KYGGKTVGKL
110 120 130 140 150
VVKDRGEEWI EEGRGNDFSK ASKRSGGEGF SSMMYRVARN STLQYPNKFI
160 170 180 190 200
GPEKCGECHP AQYETWSRSR HATTIRFPGE HPEVNNKLND PVFDKDTASI
210 220 230 240 250
LPQGITPDVV YCTVGHIRTK FGFFDAWLLR GTYHVEGGLL KNGTGQIVAG
260 270 280 290 300
GNQWQRTWAL NLSPEVAKKI KKWVPDFPVT LEEYGDNGGY VRGLASYAAK
310 320 330 340 350
YKKSMSFQAS TSYCEVCHPW KFDFKNESEF YAALGNAKEL QKHTISKGVS
360 370 380 390 400
CEECHGAGGH LEGGSGLLIS NCERCHQRFS YSPDLMRNNP LNAGKPDLAL
410 420 430 440 450
SSKFKSMGPG CGSEGSQTYF TAHYEKGMRC ATCHDPHDVT GNVTGEKGIK
460 470 480 490 500
GVSYNSEQGY LSSLYSKPKL KKECTDCHKE QAYIQSKADT HSKNSCASCH
510 520 530 540 550
MPFMMSCENF YAIQFQDQAG FDTQRRAHIW KIDVDPARKS LVAGSTSKDP
560 570 580 590 600
RDGKDWHFER NEEGRNFVDL MWACARTTWA DKDQAEAKGC HSPVVSELKE
610 620 630 640 650
TLHFKDQKQV YNEVMGWQTP VKDKFTQVKV GIQGLYSLLE VKKLAPSDKT
660 670 680 690 700
RVYELIEKAQ DTVDLIEKDG SWGMHGFKYT KQRLDAAVEY INEAQRIMKK

SL
Length:702
Mass (Da):78,939
Last modified:December 15, 2003 - v1
Checksum:i7F03B02298162E28
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571658 Genomic DNA. Translation: CAE09526.1.

Genome annotation databases

EnsemblBacteriaiCAE09526; CAE09526; WS0379.
KEGGiwsu:WS0379.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiMCCA_WOLSU
AccessioniPrimary (citable) accession number: Q7MSJ8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 29, 2015
Last sequence update: December 15, 2003
Last modified: June 7, 2017
This is version 71 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families