(data stored in ACNUC7421 zone)

SWISSPROT: A8FQH2_SHESH

ID   A8FQH2_SHESH            Unreviewed;       678 AA.
AC   A8FQH2;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 59.
DE   RecName: Full=Dissimilatory sulfite reductase {ECO:0000256|HAMAP-Rule:MF_02023};
DE            EC=1.8.99.- {ECO:0000256|HAMAP-Rule:MF_02023};
DE   Flags: Precursor;
GN   OrderedLocusNames=Ssed_0482 {ECO:0000313|EMBL:ABV35095.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV35095.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV35095.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV35095.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|HAMAP-Rule:MF_02023}.
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:0000256|HAMAP-Rule:MF_02023}.
CC   -!- COFACTOR:
CC       Name=Cu(+); Xref=ChEBI:CHEBI:49552; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02023};
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:0000256|HAMAP-Rule:MF_02023};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02023};
CC       Note=Binds 8 heme groups covalently per monomer.
CC       {ECO:0000256|HAMAP-Rule:MF_02023};
CC   -!- PATHWAY: Sulfur metabolism; sulfite reduction. {ECO:0000256|HAMAP-
CC       Rule:MF_02023}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|HAMAP-Rule:MF_02023}.
CC   -!- SIMILARITY: Belongs to the multiheme cytochrome c family.
CC       {ECO:0000256|HAMAP-Rule:MF_02023}.
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DR   EMBL; CP000821; ABV35095.1; -; Genomic_DNA.
DR   RefSeq; WP_012140832.1; NC_009831.1.
DR   ProteinModelPortal; A8FQH2; -.
DR   STRING; 425104.Ssed_0482; -.
DR   EnsemblBacteria; ABV35095; ABV35095; Ssed_0482.
DR   KEGG; sse:Ssed_0482; -.
DR   eggNOG; ENOG4105V2T; Bacteria.
DR   eggNOG; ENOG410XSMT; LUCA.
DR   HOGENOM; HOG000286693; -.
DR   OMA; DCHEAQA; -.
DR   OrthoDB; POG091H0S4L; -.
DR   BioCyc; SSED425104:GH7Q-504-MONOMER; -.
DR   UniPathway; UPA00370; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016002; F:sulfite reductase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009061; P:anaerobic respiration; IEA:UniProtKB-KW.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_02023; Sulfite_red; 1.
DR   InterPro; IPR011031; Multihaem_cyt.
DR   InterPro; IPR010177; Paired_CXXCH_1.
DR   InterPro; IPR032897; Sulfite_reductase.
DR   Pfam; PF09699; Paired_CXXCH_1; 1.
DR   SUPFAM; SSF48695; SSF48695; 4.
DR   PROSITE; PS51008; MULTIHEME_CYTC; 2.
PE   3: Inferred from homology;
DR   PRODOM; A8FQH2.
DR   SWISS-2DPAGE; A8FQH2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Copper {ECO:0000256|HAMAP-Rule:MF_02023};
KW   Electron transport {ECO:0000256|HAMAP-Rule:MF_02023};
KW   Heme {ECO:0000256|HAMAP-Rule:MF_02023};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_02023};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02023};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02023};
KW   Periplasm {ECO:0000256|HAMAP-Rule:MF_02023};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_02023};
KW   Sulfate respiration {ECO:0000256|HAMAP-Rule:MF_02023};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_02023}.
FT   SIGNAL        1     24       {ECO:0000256|HAMAP-Rule:MF_02023}.
FT   CHAIN        25    678       Dissimilatory sulfite reductase.
FT                                {ECO:0000256|HAMAP-Rule:MF_02023}.
FT                                /FTId=PRO_5009007188.
FT   DOMAIN      136    150       Cytochrome c. {ECO:0000259|PROSITE:
FT                                PS51008}.
FT   DOMAIN      297    475       Cytochrome c. {ECO:0000259|PROSITE:
FT                                PS51008}.
FT   METAL       145    145       Iron (heme 1 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       157    157       Iron (heme 4 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       306    306       Iron (heme 2 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       343    343       Iron (heme 3 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       348    348       Iron (heme 1 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       364    364       Iron (heme 4 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       398    398       Copper. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       410    410       Iron (heme 6 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       421    421       Iron (heme 5 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       424    424       Iron (heme 3 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       448    448       Iron (heme 6 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       461    461       Iron (heme 8 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       470    470       Iron (heme 7 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       477    477       Copper. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       498    498       Iron (heme 5 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       561    561       Iron (heme 8 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       645    645       Iron (heme 7 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   BINDING     141    141       Heme 1 (covalent). {ECO:0000256|HAMAP-
FT                                Rule:MF_02023}.
FT   BINDING     144    144       Heme 1 (covalent). {ECO:0000256|HAMAP-
FT                                Rule:MF_02023}.
FT   BINDING     208    208       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   BINDING     285    285       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   BINDING     302    302       Heme 2 (covalent). {ECO:0000256|HAMAP-
FT                                Rule:MF_02023}.
FT   BINDING     305    305       Heme 2 (covalent). {ECO:0000256|HAMAP-
FT                                Rule:MF_02023}.
FT   BINDING     339    339       Heme 3 (covalent). {ECO:0000256|HAMAP-
FT                                Rule:MF_02023}.
FT   BINDING     342    342       Heme 3 (covalent). {ECO:0000256|HAMAP-
FT                                Rule:MF_02023}.
FT   BINDING     360    360       Heme 4 (covalent). {ECO:0000256|HAMAP-
FT                                Rule:MF_02023}.
FT   BINDING     363    363       Heme 4 (covalent). {ECO:0000256|HAMAP-
FT                                Rule:MF_02023}.
FT   BINDING     366    366       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   BINDING     417    417       Heme 5 (covalent). {ECO:0000256|HAMAP-
FT                                Rule:MF_02023}.
FT   BINDING     420    420       Heme 5 (covalent). {ECO:0000256|HAMAP-
FT                                Rule:MF_02023}.
FT   BINDING     444    444       Heme 6 (covalent). {ECO:0000256|HAMAP-
FT                                Rule:MF_02023}.
FT   BINDING     447    447       Heme 6 (covalent). {ECO:0000256|HAMAP-
FT                                Rule:MF_02023}.
FT   BINDING     466    466       Heme 7 (covalent). {ECO:0000256|HAMAP-
FT                                Rule:MF_02023}.
FT   BINDING     469    469       Heme 7 (covalent). {ECO:0000256|HAMAP-
FT                                Rule:MF_02023}.
FT   BINDING     544    544       Heme 8 (covalent). {ECO:0000256|HAMAP-
FT                                Rule:MF_02023}.
FT   BINDING     560    560       Heme 8 (covalent). {ECO:0000256|HAMAP-
FT                                Rule:MF_02023}.
SQ   SEQUENCE   678 AA;  75778 MW;  DACE508159CE03B4 CRC64;
     MKNWKLKTAA GLLFCFTAAA NVNAAGGKYN SVPEMGESAK AAIANYQGTE ETKGVKSLHD
     YVVQESELFD FLFQNHPMFK YHEEGNLIGE YHISDRGEEY FDTGNSPKYS ERVGRPSAVQ
     YRLGAKSTLD FPNNFVGPEK CGECHAVQYE KWQRSRHANV VRFPSEITDK EVPNGDLTAR
     LYGSEAAMLP DGIQPDDVYA IIGTPRTKYG LLDSYLVRGT YHIRDGLLSE GTGKMVAGAN
     QFSRGWAEWL TPEMAKKINK VIPEFPTTIE GFGASGSHQW GMSSYGAKYE KEMLFQPASS
     YCEMCHTFKF DFQNKEEYFA ALGDSKKLQE HTISKGIACE ECHGAGGHLD GGTGGMQSNC
     ERCHQRFNFV DELADTEKGQ EKMEYAFGVK MKSACPSCGT EGSQMFASAH YEKGMRCTTC
     HDPHEVTDGD FLSGFTKPKL KKDCVDCHEA QATIADNTDT HSNQTCQSCH MPAMGSCENF
     TAVQFPDMAG FDAVRKSHMW KIDIHPERKT LNPPEGKPRD SAVKGWTVAK NEEDRNYLDL
     MWSCARTSVS DHDNVENKGC HSPFQSELET GMHYNDQMEI YGEVMKWQTP VKEVYAQVEQ
     ALVRIDQLLE VTKLPTEEKT QVLMLAEKAQ EAVDLIKKDG SWGVHGFRYS QKRLDAALTY
     VTQAQKILDG NGYSAKAN
//

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