(data stored in SCRATCH zone)

SWISSPROT: A8FQI3_SHESH

ID   A8FQI3_SHESH            Unreviewed;       676 AA.
AC   A8FQI3;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 61.
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_0493 {ECO:0000313|EMBL:ABV35106.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV35106.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV35106.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV35106.1,
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; ABV35106.1; -; Genomic_DNA.
DR   RefSeq; WP_012140843.1; NC_009831.1.
DR   ProteinModelPortal; A8FQI3; -.
DR   STRING; 425104.Ssed_0493; -.
DR   EnsemblBacteria; ABV35106; ABV35106; Ssed_0493.
DR   KEGG; sse:Ssed_0493; -.
DR   eggNOG; ENOG4105V2T; Bacteria.
DR   eggNOG; ENOG410XSMT; LUCA.
DR   HOGENOM; HOG000286693; -.
DR   OMA; EHPEVDN; -.
DR   OrthoDB; POG091H0S4L; -.
DR   BioCyc; SSED425104:GH7Q-515-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; IPR023155; Cyt_c-552/4.
DR   InterPro; IPR011031; Multihaem_cyt.
DR   InterPro; IPR032897; Sulfite_reductase.
DR   Pfam; PF13435; Cytochrome_C554; 1.
DR   SUPFAM; SSF48695; SSF48695; 3.
DR   PROSITE; PS51008; MULTIHEME_CYTC; 2.
PE   3: Inferred from homology;
DR   PRODOM; A8FQI3.
DR   SWISS-2DPAGE; A8FQI3.
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    676       Dissimilatory sulfite reductase.
FT                                {ECO:0000256|HAMAP-Rule:MF_02023}.
FT                                /FTId=PRO_5009007184.
FT   DOMAIN      135    149       Cytochrome c. {ECO:0000259|PROSITE:
FT                                PS51008}.
FT   DOMAIN      294    472       Cytochrome c. {ECO:0000259|PROSITE:
FT                                PS51008}.
FT   METAL       144    144       Iron (heme 1 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       156    156       Iron (heme 4 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       303    303       Iron (heme 2 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       340    340       Iron (heme 3 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       345    345       Iron (heme 1 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       361    361       Iron (heme 4 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       395    395       Copper. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       407    407       Iron (heme 6 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       418    418       Iron (heme 5 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       421    421       Iron (heme 3 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       445    445       Iron (heme 6 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       458    458       Iron (heme 8 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       467    467       Iron (heme 7 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       474    474       Copper. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   METAL       495    495       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     140    140       Heme 1 (covalent). {ECO:0000256|HAMAP-
FT                                Rule:MF_02023}.
FT   BINDING     143    143       Heme 1 (covalent). {ECO:0000256|HAMAP-
FT                                Rule:MF_02023}.
FT   BINDING     205    205       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   BINDING     282    282       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   BINDING     299    299       Heme 2 (covalent). {ECO:0000256|HAMAP-
FT                                Rule:MF_02023}.
FT   BINDING     302    302       Heme 2 (covalent). {ECO:0000256|HAMAP-
FT                                Rule:MF_02023}.
FT   BINDING     336    336       Heme 3 (covalent). {ECO:0000256|HAMAP-
FT                                Rule:MF_02023}.
FT   BINDING     339    339       Heme 3 (covalent). {ECO:0000256|HAMAP-
FT                                Rule:MF_02023}.
FT   BINDING     357    357       Heme 4 (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       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02023}.
FT   BINDING     414    414       Heme 5 (covalent). {ECO:0000256|HAMAP-
FT                                Rule:MF_02023}.
FT   BINDING     417    417       Heme 5 (covalent). {ECO:0000256|HAMAP-
FT                                Rule:MF_02023}.
FT   BINDING     441    441       Heme 6 (covalent). {ECO:0000256|HAMAP-
FT                                Rule:MF_02023}.
FT   BINDING     444    444       Heme 6 (covalent). {ECO:0000256|HAMAP-
FT                                Rule:MF_02023}.
FT   BINDING     463    463       Heme 7 (covalent). {ECO:0000256|HAMAP-
FT                                Rule:MF_02023}.
FT   BINDING     466    466       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   676 AA;  75712 MW;  0A2E99AFA7E47ED3 CRC64;
     MRRWKHKVAL SVLFCFGAIA NANAAGKYDS IPQMGKTAKE SIANYQGTER INGVKTLQDY
     IVQEEELFDF LFENHPMFKY QESGNLVGDY HISDRGEEYL DTGHSPSYSK GVGKPRAVQY
     RLGAKSILDY PNNFVGPEKC AECHATQYEK WQRSRHAKTI RFPGEHPEVD NDLEQTMYGT
     KDTSILPDGV TPDAIYATVG TPRTKYGFID AWLVRGTYHI EGGLLKDGTG KMVAGANQFS
     RGWAEWLTPE MAKKINDVIP AFPTTIEAFG ASGSHQKGMS SYGAKYREAM LFQPASSYCE
     ICHTFKFDFQ SKQEYFDALG DPKKLQEHTI SKGIACEECH GAGGHLDGGT GGMQSNCERC
     HQRFQYDPTL QDTPEAQEKG EYAFGVKMKS LCPSCGTEGS QMYNSEHYEK GMRCTTCHDP
     HEVTDGTWMS GITKPKLKKD CQDCHEAQTL IASNTDTHSE QTCQSCHMPN MGSCENFKAM
     QFPDQAGFDA VRKSHMWKID VDPVRKTINP PEGEPRTQGP DGGKGWTVAK NEEGRSYLDL
     MWSCARTAIS DHDVVENKGC HSQFQSELEV GLHYEDQKEI YGEVMKMQTP VKEVYAKVEQ
     ALERIDQLLE VTKLSVEDKT QVLMLAEKAE ETVNLVKKDG SWGVHGFRYT QKRLDAALTY
     VTQAQNILDG TGYAAK
//

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