ID E1SQS3_FERBD Unreviewed; 672 AA.
AC E1SQS3;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
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=Fbal_1667 {ECO:0000313|EMBL:ADN75871.1};
OS Ferrimonas balearica (strain DSM 9799 / CCM 4581 / KCTC 23876 / PAT).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Ferrimonadaceae; Ferrimonas.
OX NCBI_TaxID=550540 {ECO:0000313|EMBL:ADN75871.1, ECO:0000313|Proteomes:UP000006683};
RN [1] {ECO:0000313|EMBL:ADN75871.1, ECO:0000313|Proteomes:UP000006683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9799 / CCM 4581 / KCTC 23876 / PAT
RC {ECO:0000313|Proteomes:UP000006683};
RX DOI=10.4056/sigs.1161239;
RA Nolan M., Sikorski J., Davenport K., Lucas S., Glavina Del Rio T., Tice H.,
RA Cheng J., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y., Jeffries C., Tapia R., Brettin T., Detter J., Han C.,
RA Yasawong M., Rohde M., Tindall B., Goker M., Woyke T., Bristow J.,
RA Eisen J., Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Lapidus A.;
RT "Complete genome sequence of Ferrimonas balearica type strain (PAT).";
RL Stand. Genomic Sci. 3:174-182(2010).
CC -!- FUNCTION: Respiratory sulfite reductase that catalyzes the reduction of
CC sulfite to sulfide in a single step, consuming six electrons in the
CC process. {ECO:0000256|HAMAP-Rule:MF_02023}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-disulfide + 2 A + 3 H2O + hydrogen sulfide =
CC [protein]-dithiol + 2 AH2 + H(+) + sulfite; Xref=Rhea:RHEA:51676,
CC Rhea:RHEA-COMP:10593, Rhea:RHEA-COMP:10594, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:29919, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:50058; Evidence={ECO:0000256|HAMAP-Rule:MF_02023};
CC -!- COFACTOR:
CC Name=Cu(+); Xref=ChEBI:CHEBI:49552;
CC Evidence={ECO:0000256|HAMAP-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 bind
CC the copper ion. {ECO:0000256|HAMAP-Rule:MF_02023};
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02023};
CC Note=Binds 8 heme c groups covalently per monomer. {ECO:0000256|HAMAP-
CC 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; CP002209; ADN75871.1; -; Genomic_DNA.
DR RefSeq; WP_013345177.1; NC_014541.1.
DR AlphaFoldDB; E1SQS3; -.
DR STRING; 550540.Fbal_1667; -.
DR GeneID; 67181875; -.
DR KEGG; fbl:Fbal_1667; -.
DR eggNOG; COG0484; Bacteria.
DR HOGENOM; CLU_406457_0_0_6; -.
DR OrthoDB; 9814800at2; -.
DR UniPathway; UPA00370; -.
DR Proteomes; UP000006683; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016002; F:sulfite reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009061; P:anaerobic respiration; IEA:UniProtKB-KW.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.10.10; Cytochrome C3; 1.
DR HAMAP; MF_02023; Sulfite_red; 1.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR InterPro; IPR010177; Paired_CXXCH_1.
DR InterPro; IPR032897; Sulfite_reductase.
DR PANTHER; PTHR35038:SF6; CYTOCHROME C-TYPE PROTEIN NRFB; 1.
DR PANTHER; PTHR35038; DISSIMILATORY SULFITE REDUCTASE SIRA; 1.
DR Pfam; PF09699; Paired_CXXCH_1; 1.
DR SUPFAM; SSF48695; Multiheme cytochromes; 1.
PE 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000006683};
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..23
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT CHAIN 24..672
FT /note="Dissimilatory sulfite reductase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT /id="PRO_5009010575"
FT DOMAIN 411..448
FT /note="Doubled CXXCH motif"
FT /evidence="ECO:0000259|Pfam:PF09699"
FT REGION 503..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 141
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 144
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 145
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 157
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 300
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 303
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 304
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 337
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 340
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 341
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 346
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 358
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 361
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 362
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 394
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 406
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="6"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 413
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 416
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 417
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 420
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 440
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="6"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 443
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="6"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 444
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="6"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 457
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="8"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 462
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="7"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 465
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="7"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 466
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="7"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 473
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 494
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 540
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="8"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 556
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="8"
FT /note="covalent"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 557
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="8"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
FT BINDING 641
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="7"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02023"
SQ SEQUENCE 672 AA; 74598 MW; 30B8D83009C41937 CRC64;
MKTWKLRATV AAVIATTSVA AYAGDAAKGP NPKMSPQAQL IFNNPDGTEA VKGVKTLHDY
IVDEKELFEF LFENHPIFKT YGPENRMLGT PHISDRGEEY LHTGNSEEYS GVVGRPSAVQ
YRLGSKSILD YPNKFVGPEK CGECHQVQYE KWKRSRHANT IRFPEHVVEA PNGDLNAGLY
GTEASILPMG ITEDAIYAVV GTPRTKYGFI DPYLVRGSYH IVDGLLKDGT GTLVAGGNQF
SRVWAEWLTP EMAKKINKVI PDFPVDMAEH GKMGSNVWGM NSYGSTYKDK LLFQPASSYC
EVCHTFKFDF QSDDEFFAAL GNPEELRKHT IARGVSCEEC HGAGAHLDGG VGKLQSNCER
CHQRFDYKPQ IATGPDAKPE DAFGVKMKGA CPSCGTEGSQ MFGSAHYDAG MRCTTCHDPH
EVTDGNYLTG VTKTNQKMEC GSCHEAQAEF HAQSQAHGES DCTSCHMPNM GSCEKFKSIQ
FPDHAGFDNV RASHVWNIDV HPNRKTLNPG EGQPRDGSGK DWTMAKDEDG YTYLDLMWSC
ARTSSSDRNV VNGKGCHSQF QSELDEGLHF QDQMEIYGEV MKWQEPVKET HAKVVKSIER
IEQLLNVTRL STSDKAQILM MVDKARDAVA KIETDGSWGV HSFDYSKRII EDAWIYVQEA
QAMLDAGDYV GE
//
