CYC3_MEGG1
ID CYC3_MEGG1 Reviewed; 112 AA.
AC P00133;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Cytochrome c3;
OS Megalodesulfovibrio gigas (strain ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM
OS B-1759) (Desulfovibrio gigas).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Megalodesulfovibrio.
OX NCBI_TaxID=1121448;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM B-1759;
RX PubMed=11947254; DOI=10.1016/0014-5793(69)80308-x;
RA Ambler R.P., Bruschi M., le Gall J.;
RT "The structure of cytochrome c'-3 from Desulfovibrio gigas (NCIB 9332).";
RL FEBS Lett. 5:115-117(1969).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RA Kissinger C.;
RL Thesis (1989), University of Seattle, United States.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND SEQUENCE REVISION TO 21.
RX PubMed=8819167; DOI=10.1002/pro.5560050713;
RA Matias P.M., Morais J., Coelho R., Carrondo M.A., Wilson K., Dauter Z.,
RA Sieker L.;
RT "Cytochrome c3 from Desulfovibrio gigas: crystal structure at 1.8-A
RT resolution and evidence for a specific calcium-binding site.";
RL Protein Sci. 5:1342-1354(1996).
CC -!- FUNCTION: Participates in sulfate respiration coupled with
CC phosphorylation by transferring electrons from the enzyme dehydrogenase
CC to ferredoxin.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:8819167};
CC Note=Binds 4 heme c groups covalently per monomer.
CC {ECO:0000269|PubMed:8819167};
CC -!- MISCELLANEOUS: The second and fourth heme binding sites have unusual
CC CXXXXCH motifs. {ECO:0000269|PubMed:8819167, ECO:0007744|PDB:1WAD}.
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DR PIR; A00126; CCDV3G.
DR PDB; 1QN0; NMR; -; A=1-112.
DR PDB; 1QN1; NMR; -; A=1-112.
DR PDB; 1WAD; X-ray; 1.80 A; A=1-112.
DR PDBsum; 1QN0; -.
DR PDBsum; 1QN1; -.
DR PDBsum; 1WAD; -.
DR AlphaFoldDB; P00133; -.
DR BMRB; P00133; -.
DR SMR; P00133; -.
DR STRING; 1121448.DGI_0144; -.
DR EvolutionaryTrace; P00133; -.
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.
DR PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW Metal-binding; Sulfate respiration; Transport.
FT CHAIN 1..112
FT /note="Cytochrome c3"
FT /id="PRO_0000108360"
FT BINDING 26
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:0007744|PDB:1QN0, ECO:0007744|PDB:1QN1,
FT ECO:0007744|PDB:1WAD"
FT BINDING 29
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:0007744|PDB:1QN1, ECO:0007744|PDB:1WAD"
FT BINDING 34
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1QN0, ECO:0007744|PDB:1QN1,
FT ECO:0007744|PDB:1WAD"
FT BINDING 37
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1QN0, ECO:0007744|PDB:1QN1,
FT ECO:0007744|PDB:1WAD"
FT BINDING 38
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:0007744|PDB:1QN0, ECO:0007744|PDB:1QN1,
FT ECO:0007744|PDB:1WAD"
FT BINDING 39
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:0007744|PDB:1QN0, ECO:0007744|PDB:1QN1,
FT ECO:0007744|PDB:1WAD"
FT BINDING 49
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1QN0, ECO:0007744|PDB:1QN1,
FT ECO:0007744|PDB:1WAD"
FT BINDING 54
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1QN0, ECO:0007744|PDB:1QN1,
FT ECO:0007744|PDB:1WAD"
FT BINDING 55
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:0007744|PDB:1QN0, ECO:0007744|PDB:1QN1,
FT ECO:0007744|PDB:1WAD"
FT BINDING 73
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:0007744|PDB:1QN0, ECO:0007744|PDB:1QN1,
FT ECO:0007744|PDB:1WAD"
FT BINDING 83
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1QN0, ECO:0007744|PDB:1QN1,
FT ECO:0007744|PDB:1WAD"
FT BINDING 86
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1QN0, ECO:0007744|PDB:1QN1,
FT ECO:0007744|PDB:1WAD"
FT BINDING 87
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:0007744|PDB:1QN1, ECO:0007744|PDB:1WAD"
FT BINDING 104
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1QN0, ECO:0007744|PDB:1QN1,
FT ECO:0007744|PDB:1WAD"
FT BINDING 109
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1QN0, ECO:0007744|PDB:1QN1,
FT ECO:0007744|PDB:1WAD"
FT BINDING 110
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:0007744|PDB:1QN0, ECO:0007744|PDB:1QN1,
FT ECO:0007744|PDB:1WAD"
FT CONFLICT 21
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:1WAD"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:1WAD"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:1WAD"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:1WAD"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:1WAD"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:1QN1"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1QN1"
FT HELIX 68..73
FT /evidence="ECO:0007829|PDB:1WAD"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:1WAD"
FT HELIX 95..102
FT /evidence="ECO:0007829|PDB:1WAD"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:1WAD"
SQ SEQUENCE 112 AA; 11978 MW; 61FF10231F4C0080 CRC64;
VDVPADGAKI DFIAGGEKNL TVVFNHSTHK DVKCDDCHHD PGDKQYAGCT TDGCHNILDK
ADKSVNSWYK VVHDAKGGAK PTCISCHKDK AGDDKELKKK LTGCKGSACH PS
