CYC32_DESNO
ID CYC32_DESNO Reviewed; 111 AA.
AC P38554;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Cytochrome c3, 26 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.
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 [2]
RP PROTEIN SEQUENCE OF 1-30.
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 [3]
RP X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS).
RX PubMed=8740362; DOI=10.1016/s0969-2126(96)00045-7;
RA Czjek M., Guerlesquin F., Bruschi M., Haser R.;
RT "Crystal structure of a dimeric octaheme cytochrome c3 (M(r) 26,000) from
RT Desulfovibrio desulfuricans Norway.";
RL Structure 4:395-404(1996).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT GLU-73.
RX PubMed=9485359; DOI=10.1021/bi971656g;
RA Aubert C., Giudici-Orticoni M.-T., Czjzek M., Haser R., Bruschi M.,
RA Dolla A.;
RT "Structural and kinetic studies of the Y73E mutant of octaheme cytochrome
RT c3 (Mr = 26 000) from Desulfovibrio desulfuricans Norway.";
RL Biochemistry 37:2120-2130(1998).
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 c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000269|PubMed:8740362};
CC Note=Binds 4 heme c groups covalently per monomer.
CC {ECO:0000269|PubMed:8740362};
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- MISCELLANEOUS: The second heme binding site has an unusual CXXXXCH
CC motif. {ECO:0000269|PubMed:8740362}.
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DR PIR; S43400; S43400.
DR PDB; 1AQE; X-ray; 2.20 A; A=1-111.
DR PDB; 1CZJ; X-ray; 2.16 A; A=1-111.
DR PDBsum; 1AQE; -.
DR PDBsum; 1CZJ; -.
DR AlphaFoldDB; P38554; -.
DR SMR; P38554; -.
DR STRING; 52561.SAMN05421830_11426; -.
DR EvolutionaryTrace; P38554; -.
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; Sulfate respiration; Transport.
FT CHAIN 1..111
FT /note="Cytochrome c3, 26 kDa"
FT /id="PRO_0000108359"
FT BINDING 30
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:0000269|PubMed:8740362,
FT ECO:0007744|PDB:1AQE, ECO:0007744|PDB:1CZJ"
FT BINDING 33
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:0000269|PubMed:8740362,
FT ECO:0007744|PDB:1AQE, ECO:0007744|PDB:1CZJ"
FT BINDING 38
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:8740362,
FT ECO:0007744|PDB:1AQE, ECO:0007744|PDB:1CZJ"
FT BINDING 41
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:8740362,
FT ECO:0007744|PDB:1AQE, ECO:0007744|PDB:1CZJ"
FT BINDING 42
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:0000269|PubMed:8740362,
FT ECO:0007744|PDB:1AQE, ECO:0007744|PDB:1CZJ"
FT BINDING 43
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:0000269|PubMed:8740362,
FT ECO:0007744|PDB:1AQE, ECO:0007744|PDB:1CZJ"
FT BINDING 54
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:8740362,
FT ECO:0007744|PDB:1AQE, ECO:0007744|PDB:1CZJ"
FT BINDING 59
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:8740362,
FT ECO:0007744|PDB:1AQE, ECO:0007744|PDB:1CZJ"
FT BINDING 60
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:0000269|PubMed:8740362,
FT ECO:0007744|PDB:1AQE, ECO:0007744|PDB:1CZJ"
FT BINDING 77
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:0000269|PubMed:8740362,
FT ECO:0007744|PDB:1AQE, ECO:0007744|PDB:1CZJ"
FT BINDING 86
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:8740362,
FT ECO:0007744|PDB:1AQE, ECO:0007744|PDB:1CZJ"
FT BINDING 89
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:8740362,
FT ECO:0007744|PDB:1AQE, ECO:0007744|PDB:1CZJ"
FT BINDING 90
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:0000269|PubMed:8740362,
FT ECO:0007744|PDB:1AQE, ECO:0007744|PDB:1CZJ"
FT BINDING 105
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:8740362,
FT ECO:0007744|PDB:1AQE, ECO:0007744|PDB:1CZJ"
FT BINDING 108
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:8740362,
FT ECO:0007744|PDB:1AQE, ECO:0007744|PDB:1CZJ"
FT BINDING 109
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:0000269|PubMed:8740362,
FT ECO:0007744|PDB:1AQE, ECO:0007744|PDB:1CZJ"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:1CZJ"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1AQE"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:1CZJ"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:1CZJ"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:1CZJ"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:1CZJ"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:1CZJ"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1AQE"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1CZJ"
FT HELIX 72..77
FT /evidence="ECO:0007829|PDB:1CZJ"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1CZJ"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:1CZJ"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:1CZJ"
SQ SEQUENCE 111 AA; 12522 MW; 0F584BE53FD4CE4E CRC64;
ETFEIPESVT MSPKQFEGYT PKKGDVTFNH ASHMDIACQQ CHHTVPDTYT IESCMTEGCH
DNIKERTEIS SVYRTFHTTK DSEKSCVGCH RELKRQGPSD APLACNSCHV Q
