CYC3_DESVH
ID CYC3_DESVH Reviewed; 129 AA.
AC P00131; P81150;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Cytochrome c3;
DE Flags: Precursor;
GN OrderedLocusNames=DVU_3171;
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=882;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3019687; DOI=10.1111/j.1432-1033.1986.tb09874.x;
RA Voordouw G., Brenner S.;
RT "Cloning and sequencing of the gene encoding cytochrome c3 from
RT Desulfovibrio vulgaris (Hildenborough).";
RL Eur. J. Biochem. 159:347-351(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA Wall J.D., Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
RN [3]
RP PROTEIN SEQUENCE OF 23-129.
RX PubMed=4358550; DOI=10.1016/s0021-9258(19)43042-1;
RA Trousil E.B., Campbell L.L.;
RT "Amino acid sequence of cytochrome c3 from Desulfovibrio vulgaris.";
RL J. Biol. Chem. 249:386-393(1974).
RN [4]
RP PROTEIN SEQUENCE OF 23-44.
RX PubMed=8388770; DOI=10.1139/m93-059;
RA Kwoh D.Y., Vedvick T.S., McCue A.F., Gevertz D.;
RT "Rapid comparison of the cytochrome c3 gene from nine strains of
RT Desulfovibrio vulgaris using polymerase chain reaction amplification.";
RL Can. J. Microbiol. 39:402-411(1993).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=1663945; DOI=10.1093/oxfordjournals.jbchem.a123615;
RA Morimoto Y., Tani T., Okumura H., Higuchi Y., Yasuoka N.;
RT "Effects of amino acid substitution on three-dimensional structure: an X-
RT ray analysis of cytochrome c3 from Desulfovibrio vulgaris Hildenborough at
RT 2-A resolution.";
RL J. Biochem. 110:532-540(1991).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=8254667; DOI=10.1006/jmbi.1993.1620;
RA Matias P.M., Frazao C., Morais J., Coll M., Carrondo M.A.;
RT "Structure analysis of cytochrome c3 from Desulfovibrio vulgaris
RT Hildenborough at 1.9-A resolution.";
RL J. Mol. Biol. 234:680-699(1993).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS).
RA Simoes P., Matias P.M., Morais J., Wilson K., Dauter Z., Carrondo M.A.;
RL Submitted (JUN-1997) to the PDB data bank.
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=9890880; DOI=10.1021/bi981593h;
RA Dolla A., Arnoux P., Protasevich I., Lobachov V., Brugna M.,
RA Giudici-Orticoni M.-T., Haser R., Czjzek M., Makarov A., Bruschi M.;
RT "Key role of phenylalanine 20 in cytochrome c3: structure, stability, and
RT function studies.";
RL Biochemistry 38:33-41(1999).
RN [9]
RP STRUCTURE BY NMR.
RX PubMed=1333991; DOI=10.1016/0014-5793(92)80963-h;
RA Salgueiro C.A., Turner D.L., Santos H., Legall J., Xavier A.V.;
RT "Assignment of the redox potentials to the four haems in Desulfovibrio
RT vulgaris cytochrome c3 by 2D-NMR.";
RL FEBS Lett. 314:155-158(1992).
RN [10]
RP STRUCTURE BY NMR.
RX PubMed=9710542; DOI=10.1006/jmbi.1998.1974;
RA Messias A.C., Kastrau D.H.W., Costa H.S., Legall J., Turner D.L.,
RA Santos H., Xavier A.V.;
RT "Solution structure of Desulfovibrio vulgaris (Hildenborough)
RT ferrocytochrome c3: structural basis for functional cooperativity.";
RL J. Mol. Biol. 281:719-739(1998).
CC -!- FUNCTION: Participates in sulfate respiration coupled with
CC phosphorylation by transferring electrons from the enzyme dehydrogenase
CC to ferredoxin.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Binds 4 heme c groups per subunit.
CC -!- MISCELLANEOUS: The second and fourth heme binding sites have unusual
CC CXXXXCH motifs.
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DR EMBL; X04304; CAA27847.1; -; Genomic_DNA.
DR EMBL; AE017285; AAS97641.1; -; Genomic_DNA.
DR PIR; A24799; CCDV3.
DR RefSeq; WP_010940429.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_012381.1; NC_002937.3.
DR PDB; 1A2I; NMR; -; A=23-129.
DR PDB; 1GX7; NMR; -; E=23-129.
DR PDB; 1MDV; X-ray; 2.30 A; A/B=23-129.
DR PDB; 2BPN; NMR; -; A=23-129.
DR PDB; 2CTH; X-ray; 1.67 A; A/B=23-129.
DR PDB; 2CYM; X-ray; 2.00 A; A=23-129.
DR PDBsum; 1A2I; -.
DR PDBsum; 1GX7; -.
DR PDBsum; 1MDV; -.
DR PDBsum; 2BPN; -.
DR PDBsum; 2CTH; -.
DR PDBsum; 2CYM; -.
DR AlphaFoldDB; P00131; -.
DR BMRB; P00131; -.
DR SMR; P00131; -.
DR STRING; 882.DVU_3171; -.
DR PaxDb; P00131; -.
DR PRIDE; P00131; -.
DR EnsemblBacteria; AAS97641; AAS97641; DVU_3171.
DR KEGG; dvu:DVU_3171; -.
DR PATRIC; fig|882.5.peg.2876; -.
DR eggNOG; ENOG503407D; Bacteria.
DR HOGENOM; CLU_125874_3_0_7; -.
DR OMA; KELTGCK; -.
DR EvolutionaryTrace; P00131; -.
DR Proteomes; UP000002194; Chromosome.
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.
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; Periplasm; Reference proteome; Signal; Sulfate respiration;
KW Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:4358550,
FT ECO:0000269|PubMed:8388770"
FT CHAIN 23..129
FT /note="Cytochrome c3"
FT /evidence="ECO:0000269|PubMed:3019687"
FT /id="PRO_0000006504"
FT BINDING 44
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 47
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 52
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT BINDING 55
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT BINDING 56
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 57
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 68
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT BINDING 73
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT BINDING 74
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 92
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 101
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT BINDING 104
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT BINDING 105
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 122
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT BINDING 127
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT BINDING 128
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:2CTH"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:2CTH"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:2CTH"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:2CTH"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:2BPN"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:2CTH"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:2BPN"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:2BPN"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:1A2I"
FT HELIX 87..92
FT /evidence="ECO:0007829|PDB:2CTH"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:1A2I"
FT HELIX 101..109
FT /evidence="ECO:0007829|PDB:2CTH"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:2CTH"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:2CTH"
SQ SEQUENCE 129 AA; 13976 MW; 78C2A85F33B18441 CRC64;
MRKLFFCGVL ALAVAFALPV VAAPKAPADG LKMEATKQPV VFNHSTHKSV KCGDCHHPVN
GKEDYRKCGT AGCHDSMDKK DKSAKGYYHV MHDKNTKFKS CVGCHVEVAG ADAAKKKDLT
GCKKSKCHE
