CYCX_DESDA
ID CYCX_DESDA Reviewed; 279 AA.
AC P81040; B8J401; Q84I46;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Split-Soret cytochrome c;
DE Flags: Precursor;
GN OrderedLocusNames=Ddes_2150;
OS Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=525146;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IRON-SULFUR CLUSTER.
RA Abreu I.A., Saraiva L.M.;
RT "Desulfovibrio desulfuricans split soret cytochrome c gene.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27774 / DSM 6949 / MB;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Hazen T.C.;
RT "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str.
RT ATCC 27774.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 33-279, AND BLOCKAGE OF N-TERMINUS.
RX PubMed=9346301; DOI=10.1111/j.1432-1033.1997.00445.x;
RA Devreese B., Costa C., Demol H., Papaefthymiou V., Moura I., Moura J.J.G.,
RA van Beeumen J.;
RT "The primary structure of the split-Soret cytochrome c from Desulfovibrio
RT desulfuricans ATCC 27774 reveals an unusual type of diheme cytochrome c.";
RL Eur. J. Biochem. 248:445-451(1997).
RN [4]
RP PROTEIN SEQUENCE OF 33-54.
RX PubMed=1646022; DOI=10.1016/s0005-2728(05)80270-1;
RA Moura J.J.G., Costa C., Liu M.Y., Moura I., Legall J.;
RT "Structural and functional approach toward a classification of the complex
RT cytochrome c system found in sulfate-reducing bacteria.";
RL Biochim. Biophys. Acta 1058:61-66(1991).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 33-279.
RA Matias P.M., Morais J., Coelho A.V., Meijers R., Gonzalez A.,
RA Thompson A.W., Sieker L., Legall J., Carrondo M.A.;
RT "A preliminary analysis of the three-dimensional structure of dimeric di-
RT haem split-Soret cytochrome c from Desulfovibrio desulfuricans ATCC 27774
RT at 2.5-A resolution using the MAD phasing method: a novel cytochrome fold
RT with a stacked-haem arrangement.";
RL J. Biol. Inorg. Chem. 2:507-514(1997).
RN [6] {ECO:0007744|PDB:1H21}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 33-279 IN COMPLEX WITH HEMES C,
RP AND COFACTOR.
RX PubMed=12589573; DOI=10.1007/s00775-002-0426-3;
RA Abreu I.A., Lourenco A.I., Xavier A.V., LeGall J., Coelho A.V.,
RA Matias P.M., Pinto D.M., Armenia Carrondo M., Teixeira M., Saraiva L.M.;
RT "A novel iron centre in the split-Soret cytochrome c from Desulfovibrio
RT desulfuricans ATCC 27774.";
RL J. Biol. Inorg. Chem. 8:360-370(2003).
CC -!- FUNCTION: Diheme cytochrome c which may be involved in sulfate
CC reduction.
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000269|PubMed:12589573};
CC Note=Binds 2 heme c groups per subunit. Each heme is also bound by the
CC other subunit. {ECO:0000269|PubMed:12589573};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Note=Binds 1 iron-sulfur cluster per subunit, probably [2Fe-2S]
CC cluster.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) are -168 mV and -330 mV.;
CC -!- SUBUNIT: Homodimer; linked through the 4 hemes that are shared between
CC the subunits.
CC -!- PTM: The N-terminal Gly is blocked by a labile group with a mass of 85
CC Da.
CC -!- PTM: Predicted to be exported by the Tat system. {ECO:0000250}.
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DR EMBL; AF465622; AAO20874.1; -; Genomic_DNA.
DR EMBL; CP001358; ACL50046.1; -; Genomic_DNA.
DR RefSeq; WP_015939155.1; NC_011883.1.
DR PDB; 1H21; X-ray; 2.50 A; A/B/C/D=33-279.
DR PDBsum; 1H21; -.
DR AlphaFoldDB; P81040; -.
DR SMR; P81040; -.
DR STRING; 525146.Ddes_2150; -.
DR DrugBank; DB03317; Ferroheme C.
DR EnsemblBacteria; ACL50046; ACL50046; Ddes_2150.
DR KEGG; dds:Ddes_2150; -.
DR eggNOG; ENOG50320QR; Bacteria.
DR HOGENOM; CLU_063015_0_0_7; -.
DR OMA; MHQVFHS; -.
DR OrthoDB; 804993at2; -.
DR EvolutionaryTrace; P81040; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009061; P:anaerobic respiration; IEA:UniProtKB-KW.
DR InterPro; IPR010181; CGCAxxGCC_motif.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF09719; C_GCAxxG_C_C; 1.
DR SUPFAM; SSF48695; SSF48695; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Direct protein sequencing; Electron transport; Heme;
KW Iron; Iron-sulfur; Metal-binding; Signal; Sulfate respiration; Transport.
FT SIGNAL 1..32
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:1646022, ECO:0000269|PubMed:9346301"
FT CHAIN 33..279
FT /note="Split-Soret cytochrome c"
FT /id="PRO_0000108442"
FT BINDING 76
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000305"
FT BINDING 118
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000305"
FT BINDING 179
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000305"
FT BINDING 180
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_note="ligand shared between homodimeric partners"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue; in chain B"
FT /evidence="ECO:0000269|PubMed:12589573,
FT ECO:0007744|PDB:1H21"
FT BINDING 203
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000305"
FT BINDING 241
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="covalent; in chain A"
FT /evidence="ECO:0000269|PubMed:12589573,
FT ECO:0007744|PDB:1H21"
FT BINDING 244
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="covalent; in chain A"
FT /evidence="ECO:0000269|PubMed:12589573,
FT ECO:0007744|PDB:1H21"
FT BINDING 245
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_note="ligand shared between homodimeric partners"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue; in chain A"
FT /evidence="ECO:0000269|PubMed:12589573,
FT ECO:0007744|PDB:1H21"
FT BINDING 261
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="covalent; in chain A"
FT /evidence="ECO:0000269|PubMed:12589573,
FT ECO:0007744|PDB:1H21"
FT BINDING 264
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="covalent; in chain A"
FT /evidence="ECO:0000269|PubMed:12589573,
FT ECO:0007744|PDB:1H21"
FT BINDING 265
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_note="ligand shared between homodimeric partners"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue; in chain A"
FT /evidence="ECO:0000269|PubMed:12589573,
FT ECO:0007744|PDB:1H21"
FT BINDING 274
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain B"
FT /evidence="ECO:0000269|PubMed:12589573,
FT ECO:0007744|PDB:1H21"
FT BINDING 278
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_note="ligand shared between homodimeric partners"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue; in chain B"
FT /evidence="ECO:0000269|PubMed:12589573,
FT ECO:0007744|PDB:1H21"
FT MOD_RES 33
FT /note="Blocked amino end (Gly)"
FT CONFLICT 34
FT /note="Q -> E (in Ref. 3; AA sequence and 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="C -> Y (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="C -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:1H21"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:1H21"
FT HELIX 76..92
FT /evidence="ECO:0007829|PDB:1H21"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1H21"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:1H21"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:1H21"
FT HELIX 119..131
FT /evidence="ECO:0007829|PDB:1H21"
FT HELIX 134..150
FT /evidence="ECO:0007829|PDB:1H21"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:1H21"
FT HELIX 179..190
FT /evidence="ECO:0007829|PDB:1H21"
FT HELIX 197..224
FT /evidence="ECO:0007829|PDB:1H21"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:1H21"
FT HELIX 236..245
FT /evidence="ECO:0007829|PDB:1H21"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:1H21"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:1H21"
SQ SEQUENCE 279 AA; 29989 MW; DFC785410229936F CRC64;
MNIGRRDLIC GLGGLAVGGA MLGLGSVEAR AAGQAQPASG RFDQVGGAFG WKPHKLDPKE
CAQVAYDGYW YKGFGCGFGA FYSIVGLMGE KYGAPYNQFP FAMLEANKGG ISDWGTICGA
LYGAAATFSL FWGRKEVHPM VNELFRWYEV TKLPIFNPGD AAQGVKGDLP MSASDSVLCH
ISVSKWCYEN KIEATSKQRS ERCGRLTADA AFKAAEIINT KIDQGKDFKS TFPMQASVSS
CGECHMTKGN DANWAKGIMD CTPCHSGTAA TQNKFVNHP
