CYC3A_DESAF
ID CYC3A_DESAF Reviewed; 127 AA.
AC P94690; Q9R4E7;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Acidic 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 29-68, FUNCTION, HEME-BINDING, AND BLOCKAGE OF
RP N-TERMINUS.
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 (1.6 ANGSTROMS) OF 25-127, AND PYROGLUTAMATE
RP FORMATION AT GLN-25.
RX PubMed=10398589; DOI=10.1006/jmbi.1999.2917;
RA Noerager S., Legrand P., Pieulle L., Hatchikian C., Roth M.;
RT "Crystal structure of the oxidised and reduced acidic cytochrome c3 from
RT Desulfovibrio africanus.";
RL J. Mol. Biol. 290:881-902(1999).
CC -!- FUNCTION: Exchanges electrons specifically with the basic cytochrome
CC c3. {ECO:0000269|PubMed:8573595}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Binds 4 heme groups per subunit.
CC -!- PTM: The N-terminus is blocked.
CC -!- MASS SPECTROMETRY: Mass=13742; Mass_error=1.2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9392524};
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DR EMBL; Y09718; CAA70884.1; -; Genomic_DNA.
DR PDB; 3CAO; X-ray; 1.60 A; A=26-127.
DR PDB; 3CAR; X-ray; 1.90 A; A=26-127.
DR PDBsum; 3CAO; -.
DR PDBsum; 3CAR; -.
DR AlphaFoldDB; P94690; -.
DR SMR; P94690; -.
DR DrugBank; DB03901; 5-Oxoprolinal.
DR EvolutionaryTrace; P94690; -.
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; Pyrrolidone carboxylic acid; Signal;
KW Sulfate respiration; Transport.
FT SIGNAL 1..24
FT CHAIN 25..127
FT /note="Acidic cytochrome c3"
FT /id="PRO_0000006502"
FT BINDING 48
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 51
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 60
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT BINDING 63
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT BINDING 64
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 65
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 83
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT BINDING 86
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT BINDING 87
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 103
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 106
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT BINDING 109
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT BINDING 110
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 120
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT BINDING 123
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT BINDING 124
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT MOD_RES 25
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:10398589"
FT CONFLICT 67
FT /note="W -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:3CAO"
FT HELIX 48..55
FT /evidence="ECO:0007829|PDB:3CAO"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:3CAO"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:3CAO"
FT HELIX 98..113
FT /evidence="ECO:0007829|PDB:3CAO"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:3CAO"
SQ SEQUENCE 127 AA; 13856 MW; DE6E3B16FA4BF8B3 CRC64;
MFKHTLIALT LLAAATLFSL PAFSQEDMTH VPTDAFGKLE RPAAVFNHDE HNEKAGIESC
NACHHVWVNG VLAEDEDSVG TPCSDCHALE QDGDTPGLQD AYHQQCWGCH EKQAKGPVMC
GECHVKN
