CYC3B_DESAF
ID CYC3B_DESAF Reviewed; 140 AA.
AC P94691; Q9R4E8;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Basic cytochrome c3;
DE Flags: Precursor;
OS Desulfocurvibacter africanus (Desulfovibrio africanus).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfocurvibacter.
OX NCBI_TaxID=873;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE,
RP CHARACTERIZATION, AND MASS SPECTROMETRY.
RC STRAIN=ATCC 19996 / DSM 2603 / NCIMB 8401 / Benghazi;
RX PubMed=9392524; DOI=10.1016/s0167-4838(97)00096-4;
RA Magro V., Pieulle L., Forget N., Guigliarelli B., Petillot Y.,
RA Hatchikian E.C.;
RT "Further characterization of the two tetraheme cytochromes c3 from
RT Desulfovibiro africanus: nucleotide sequences, EPR spectroscopy and
RT biological activity.";
RL Biochim. Biophys. Acta 1342:149-163(1997).
RN [2]
RP PROTEIN SEQUENCE OF 24-78, FUNCTION, AND HEME-BINDING.
RC STRAIN=ATCC 19996 / DSM 2603 / NCIMB 8401 / Benghazi;
RX PubMed=8573595; DOI=10.1016/0005-2728(95)00129-8;
RA Pieulle L., Haladjian J., Bonicel J., Hatchikian E.C.;
RT "Biochemical studies of the c-type cytochromes of the sulfate reducer
RT Desulfovibrio africanus. Characterization of two tetraheme cytochromes c3
RT with different specificity.";
RL Biochim. Biophys. Acta 1273:51-61(1996).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 25-140 IN COMPLEX WITH CALCIUM
RP AND HEME.
RX PubMed=16226767; DOI=10.1016/j.jmb.2005.09.036;
RA Pieulle L., Morelli X., Gallice P., Lojou E., Barbier P., Czjzek M.,
RA Bianco P., Guerlesquin F., Hatchikian E.C.;
RT "The type I/type II cytochrome c3 complex: an electron transfer link in the
RT hydrogen-sulfate reduction pathway.";
RL J. Mol. Biol. 354:73-90(2005).
CC -!- FUNCTION: Exchanges electrons with [NiFe] and [Fe] hydrogenases and
CC with the acidic cytochrome c3. Participates in sulfate respiration
CC coupled with phosphorylation by transferring electrons from the enzyme
CC dehydrogenase to ferredoxin. {ECO:0000269|PubMed:8573595}.
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000269|PubMed:16226767};
CC Note=Binds 4 heme c groups covalently per monomer.
CC {ECO:0000269|PubMed:16226767};
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- MASS SPECTROMETRY: Mass=15102; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9392524};
CC -!- MISCELLANEOUS: The second heme binding site has an unusual CXXXXCH
CC motif. {ECO:0000269|PubMed:16226767, ECO:0007744|PDB:2BQ4}.
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DR EMBL; Y09717; CAA70883.1; -; Genomic_DNA.
DR PDB; 2BQ4; X-ray; 1.68 A; A/B=25-140.
DR PDBsum; 2BQ4; -.
DR AlphaFoldDB; P94691; -.
DR SMR; P94691; -.
DR EvolutionaryTrace; P94691; -.
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; Calcium; Direct protein sequencing; Electron transport; Heme;
KW Iron; Metal-binding; Periplasm; Signal; Sulfate respiration; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:8573595"
FT CHAIN 24..140
FT /note="Basic cytochrome c3"
FT /id="PRO_0000006503"
FT BINDING 34
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:16226767,
FT ECO:0007744|PDB:2BQ4"
FT BINDING 36
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:16226767,
FT ECO:0007744|PDB:2BQ4"
FT BINDING 44
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:16226767,
FT ECO:0007744|PDB:2BQ4"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:16226767,
FT ECO:0007744|PDB:2BQ4"
FT BINDING 51
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:16226767,
FT ECO:0007744|PDB:2BQ4"
FT BINDING 54
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:16226767,
FT ECO:0007744|PDB:2BQ4"
FT BINDING 64
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:16226767,
FT ECO:0007744|PDB:2BQ4"
FT BINDING 67
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:16226767,
FT ECO:0007744|PDB:2BQ4"
FT BINDING 68
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:16226767,
FT ECO:0007744|PDB:2BQ4"
FT BINDING 69
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:16226767,
FT ECO:0007744|PDB:2BQ4"
FT BINDING 80
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:16226767,
FT ECO:0007744|PDB:2BQ4"
FT BINDING 85
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:16226767,
FT ECO:0007744|PDB:2BQ4"
FT BINDING 86
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:16226767,
FT ECO:0007744|PDB:2BQ4"
FT BINDING 107
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:16226767,
FT ECO:0007744|PDB:2BQ4"
FT BINDING 114
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:16226767,
FT ECO:0007744|PDB:2BQ4"
FT BINDING 117
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:16226767,
FT ECO:0007744|PDB:2BQ4"
FT BINDING 118
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:16226767,
FT ECO:0007744|PDB:2BQ4"
FT BINDING 133
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:16226767,
FT ECO:0007744|PDB:2BQ4"
FT BINDING 136
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:16226767,
FT ECO:0007744|PDB:2BQ4"
FT BINDING 137
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:16226767,
FT ECO:0007744|PDB:2BQ4"
FT CONFLICT 66
FT /note="K -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:2BQ4"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:2BQ4"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2BQ4"
FT HELIX 52..57
FT /evidence="ECO:0007829|PDB:2BQ4"
FT HELIX 61..65
FT /evidence="ECO:0007829|PDB:2BQ4"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2BQ4"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:2BQ4"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:2BQ4"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:2BQ4"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:2BQ4"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:2BQ4"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:2BQ4"
SQ SEQUENCE 140 AA; 14975 MW; EA2A805423F416D5 CRC64;
MKKLFSMLVA AALVGTMAMA AQAVPQVPAD VVIDHLSNPN AKLEYKVKFS HKAHASLGTD
AAACQKCHHK WDGKSEIGGC ATEGCHADTT SFKATEKDPK FLMTAFHSKS PMSCQGCHKE
MKTAKKTTGP TACAQCHNQK
