CYC3_DESAC
ID CYC3_DESAC Reviewed; 68 AA.
AC P00137;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Cytochrome c3;
DE AltName: Full=Cytochrome c551.5;
DE AltName: Full=Cytochrome c7;
GN Name=cyd;
OS Desulfuromonas acetoxidans (Chloropseudomonas ethylica).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Desulfuromonadaceae; Desulfuromonas.
OX NCBI_TaxID=891;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=11946160; DOI=10.1016/0014-5793(71)80484-2;
RA Ambler R.P.;
RT "The amino acid sequence of cytochrome c551.5 (cytochrome c-7) from the
RT green photosynthetic bacterium Chloropseudomonas ethylica.";
RL FEBS Lett. 18:351-353(1971).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9546165; DOI=10.1128/aem.64.4.1308-1312.1998;
RA Aubert C., Lojou E., Bianco P., Rousset M., Durand M.C., Bruschi M.,
RA Dolla A.;
RT "The Desulfuromonas acetoxidans triheme cytochrome c7 produced in
RT Desulfovibrio desulfuricans retains its metal reductase activity.";
RL Appl. Environ. Microbiol. 64:1308-1312(1998).
RN [3]
RP CHARACTERIZATION.
RX PubMed=9030775; DOI=10.1111/j.1432-1033.1997.0474a.x;
RA Turner D.L., Costa H.S., Coutinho I.B., Legall J., Xavier A.V.;
RT "Assignment of the ligand geometry and redox potentials of the trihaem
RT ferricytochrome c3 from Desulfuromonas acetoxidans.";
RL Eur. J. Biochem. 243:474-481(1997).
RN [4]
RP STRUCTURE BY NMR, AND FUNCTION AS A METAL REDUCTASE.
RX PubMed=12119407; DOI=10.1073/pnas.152290999;
RA Assfalg M., Bertini I., Bruschi M., Michel C., Turano P.;
RT "The metal reductase activity of some multiheme cytochromes c: NMR
RT structural characterization of the reduction of chromium(VI) to
RT chromium(III) by cytochrome c7.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9750-9754(2002).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=11320307; DOI=10.1107/s0907444901003481;
RA Czjzek M., Arnoux P., Haser R., Shepard W.;
RT "Structure of cytochrome c7 from Desulfuromonas acetoxidans at 1.9 A
RT resolution.";
RL Acta Crystallogr. D 57:670-678(2001).
RN [6]
RP STRUCTURE BY NMR.
RX PubMed=8962062; DOI=10.1073/pnas.93.25.14396;
RA Banci L., Bertini I., Bruschi M., Sompornpisut P., Turano P.;
RT "NMR characterization and solution structure determination of the oxidized
RT cytochrome c7 from Desulfuromonas acetoxidans.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:14396-14400(1996).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=9760163; DOI=10.1046/j.1432-1327.1998.2560261.x;
RA Assfalg M., Banci L., Bertini I., Bruschi M., Turano P.;
RT "800 MHz 1H NMR solution structure refinement of oxidized cytochrome c7
RT from Desulfuromonas acetoxidans.";
RL Eur. J. Biochem. 256:261-270(1998).
RN [8]
RP STRUCTURE BY NMR.
RX PubMed=10561607; DOI=10.1046/j.1432-1327.1999.00904.x;
RA Assfalg M., Banci L., Bertini I., Bruschi M., Giudici-Orticoni M.-T.,
RA Turano P.;
RT "A proton-NMR investigation of the fully reduced cytochrome c7 from
RT Desulfuromonas acetoxidans: comparison between the reduced and the oxidized
RT forms.";
RL Eur. J. Biochem. 266:634-643(1999).
RN [9]
RP STRUCTURE BY NMR.
RX PubMed=11883773; DOI=10.1023/a:1014202405862;
RA Assfalg M., Bertini I., Turano P., Bruschi M., Durand M.C.,
RA Giudici-Orticoni M.-T., Dolla A.;
RT "A quick solution structure determination of the fully oxidized double
RT mutant K9-10A cytochrome c7 from Desulfuromonas acetoxidans and mechanistic
RT implications.";
RL J. Biomol. NMR 22:107-122(2002).
CC -!- FUNCTION: Participates in sulfate respiration coupled with
CC phosphorylation by transferring electrons from the enzyme dehydrogenase
CC to ferredoxin. {ECO:0000269|PubMed:12119407}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) are -140 mV, -210 mV and -240 mV.;
CC -!- PTM: Binds 3 heme groups per subunit.
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DR EMBL; AF005234; AAC46253.1; -; Genomic_DNA.
DR PIR; A00130; CCDS7.
DR PDB; 1EHJ; NMR; -; A=1-68.
DR PDB; 1F22; NMR; -; A=1-68.
DR PDB; 1HH5; X-ray; 1.90 A; A=1-68.
DR PDB; 1KWJ; NMR; -; A=1-68.
DR PDB; 1L3O; NMR; -; A=1-68.
DR PDB; 1LM2; NMR; -; A=1-68.
DR PDB; 1NEW; NMR; -; A=1-68.
DR PDBsum; 1EHJ; -.
DR PDBsum; 1F22; -.
DR PDBsum; 1HH5; -.
DR PDBsum; 1KWJ; -.
DR PDBsum; 1L3O; -.
DR PDBsum; 1LM2; -.
DR PDBsum; 1NEW; -.
DR AlphaFoldDB; P00137; -.
DR BMRB; P00137; -.
DR SMR; P00137; -.
DR DrugBank; DB03317; Ferroheme C.
DR EvolutionaryTrace; P00137; -.
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; IPR029467; Cyt_c7-like.
DR InterPro; IPR002322; Cyt_c_III.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR Pfam; PF14522; Cytochrome_C7; 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; Sulfate respiration; Transport.
FT CHAIN 1..68
FT /note="Cytochrome c3"
FT /id="PRO_0000108364"
FT BINDING 17
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 20
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 26
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT BINDING 29
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT BINDING 30
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 45
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 49
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT BINDING 52
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT BINDING 53
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 62
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT BINDING 65
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT BINDING 66
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:1HH5"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:1EHJ"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:1HH5"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:1HH5"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:1HH5"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:1KWJ"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:1HH5"
FT TURN 45..49
FT /evidence="ECO:0007829|PDB:1HH5"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:1HH5"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1HH5"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:1HH5"
SQ SEQUENCE 68 AA; 7262 MW; 6A54074BF1A5DAB8 CRC64;
ADVVTYENKK GNVTFDHKAH AEKLGCDACH EGTPAKIAID KKSAHKDACK TCHKSNNGPT
KCGGCHIK
