CYC31_DESNO
ID CYC31_DESNO Reviewed; 118 AA.
AC P00136;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Cytochrome c3, 13 kDa;
OS Desulfomicrobium norvegicum (strain DSM 1741 / NCIMB 8310) (Desulfovibrio
OS baculatus (strain Norway 4)) (Desulfovibrio desulfuricans (strain Norway
OS 4)).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfomicrobiaceae; Desulfomicrobium.
OX NCBI_TaxID=52561;
RN [1]
RP PROTEIN SEQUENCE.
RA Bruschi M.;
RT "The primary structure of the tetrahaem cytochrome C-3 from Desulfovibrio
RT desulfuricans (strain Norway 4).";
RL Biochim. Biophys. Acta 671:219-226(1981).
RN [2]
RP SEQUENCE REVISION TO 86 AND 97-99.
RX PubMed=8142476; DOI=10.1016/0167-4838(94)90100-7;
RA Bruschi M., Leroy G., Guerlesquin F., Bonicel J.;
RT "Amino-acid sequence of the cytochrome c3 (M(r) 26,000) from Desulfovibrio
RT desulfuricans Norway and a comparison with those of the other polyhemic
RT cytochromes from Desulfovibrio.";
RL Biochim. Biophys. Acta 1205:123-131(1994).
RN [3]
RP PROTEIN SEQUENCE OF 1-36.
RX PubMed=2539120; DOI=10.1016/0006-291x(89)90047-8;
RA Loutfi M., Guerlesquin F., Bianco P., Haladjian J., Bruschi M.;
RT "Comparative studies of polyhemic cytochromes c isolated from Desulfovibrio
RT vulgaris (Hildenborough) and Desulfovibrio desulfuricans (Norway).";
RL Biochem. Biophys. Res. Commun. 159:670-676(1989).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=229424; DOI=10.1038/282806a0;
RA Haser R., Pierrot M., Frey M., Payan F., Astier J.-P., Bruschi M.,
RA le Gall J.;
RT "Structure and sequence of the multihaem cytochrome c3.";
RL Nature 282:806-810(1979).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=6292223; DOI=10.1016/s0021-9258(19)45386-6;
RA Pierrot M., Haser R., Frey M., Payan F., Astier J.-P.;
RT "Crystal structure and electron transfer properties of cytochrome c3.";
RL J. Biol. Chem. 257:14341-14348(1982).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=7966289; DOI=10.1016/0022-2836(94)90039-6;
RA Czjzek M., Payan F., Guerlesquin F., Bruschi M., Haser R.;
RT "Crystal structure of cytochrome c3 from Desulfovibrio desulfuricans Norway
RT at 1.7-A resolution.";
RL J. Mol. Biol. 243:653-667(1994).
CC -!- FUNCTION: Participates in sulfate respiration coupled with
CC phosphorylation by transferring electrons from the enzyme dehydrogenase
CC to ferredoxin.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Binds 4 heme c groups per subunit.
CC -!- MISCELLANEOUS: The second heme binding site has an unusual CXXXXCH
CC motif.
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DR PIR; A00129; CCDV3N.
DR PDB; 2CY3; X-ray; 1.70 A; A=1-118.
DR PDBsum; 2CY3; -.
DR AlphaFoldDB; P00136; -.
DR SMR; P00136; -.
DR STRING; 52561.SAMN05421830_10245; -.
DR DrugBank; DB03317; Ferroheme C.
DR EvolutionaryTrace; P00136; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009061; P:anaerobic respiration; IEA:UniProtKB-KW.
DR InterPro; IPR002322; Cyt_c_III.
DR InterPro; IPR020942; Cyt_c_III_dom.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR Pfam; PF02085; Cytochrom_CIII; 1.
DR PRINTS; PR00609; CYTOCHROMEC3.
DR SUPFAM; SSF48695; SSF48695; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW Metal-binding; Periplasm; Sulfate respiration; Transport.
FT CHAIN 1..118
FT /note="Cytochrome c3, 13 kDa"
FT /id="PRO_0000108358"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 36
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 BINDING 39
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 BINDING 44
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT BINDING 47
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT BINDING 48
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 BINDING 49
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 BINDING 61
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT BINDING 66
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT BINDING 67
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 BINDING 89
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 BINDING 92
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT BINDING 95
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT BINDING 96
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 BINDING 111
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT BINDING 114
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT BINDING 115
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 STRAND 31..33
FT /evidence="ECO:0007829|PDB:2CY3"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:2CY3"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:2CY3"
FT TURN 49..56
FT /evidence="ECO:0007829|PDB:2CY3"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:2CY3"
FT HELIX 84..101
FT /evidence="ECO:0007829|PDB:2CY3"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:2CY3"
SQ SEQUENCE 118 AA; 12622 MW; B9C3E8E14EC85728 CRC64;
ADAPGDDYVI SAPEGMKAKP KGDKPGALQK TVPFPHTKHA TVECVQCHHT LEADGGAVKK
CTTSGCHDSL EFRDKANAKD IKLVENAFHT QCIDCHKALK KDKKPTGPTA CGKCHTTN
