CYC9_DESDA
ID CYC9_DESDA Reviewed; 326 AA.
AC Q9RN68; B8J3C4;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Nine-heme cytochrome c;
DE AltName: Full=9Hcc;
DE Flags: Precursor;
GN OrderedLocusNames=Ddes_2038;
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].
RX PubMed=10471375; DOI=10.1006/bbrc.1999.1238;
RA Saraiva L.M., da Costa P.N., LeGall J.;
RT "Sequencing the gene encoding Desulfovibrio desulfuricans ATCC 27774 nine-
RT heme cytochrome c.";
RL Biochem. Biophys. Res. Commun. 262:629-634(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND X-RAY CRYSTALLOGRAPHY (1.8
RP ANGSTROMS).
RX PubMed=10555582; DOI=10.1007/s007750050334;
RA Matias P.M., Saraiva L.M., Soares C.M., Coelho A.V., LeGall J.,
RA Carrondo M.A.;
RT "Nine-haem cytochrome c from Desulfovibrio desulfuricans ATCC 27774:
RT primary sequence determination, crystallographic refinement at 1.8 A and
RT modelling studies of its interaction with the tetrahaem cytochrome c3.";
RL J. Biol. Inorg. Chem. 4:478-494(1999).
RN [3]
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 [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=10368280; DOI=10.1016/s0969-2126(99)80019-7;
RA Matias P.M., Coelho R., Pereira I.A.C., Coelho A.V., Thompson A.W.,
RA Sieker L., LeGall J., Carrondo M.A.;
RT "The primary and three-dimensional structures of a nine-haem cytochrome c
RT from Desulfovibrio desulfuricans ATCC 27774 reveal a new member of the Hmc
RT family.";
RL Structure 7:119-130(1999).
CC -!- FUNCTION: May form part of a transmembrane redox complex through which
CC electrons are transferred to the cytoplasm for reduction of sulfate.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- DOMAIN: Arranged into two tetraheme clusters and the extra heme 4 is
CC located asymmetrically between the two regions.
CC -!- PTM: Binds 9 heme groups per subunit.
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DR EMBL; AF186393; AAD56586.1; -; Genomic_DNA.
DR EMBL; CP001358; ACL49934.1; -; Genomic_DNA.
DR PIR; JC7094; JC7094.
DR RefSeq; WP_012625658.1; NC_011883.1.
DR PDB; 19HC; X-ray; 1.80 A; A/B=31-321.
DR PDB; 1OFW; X-ray; 1.50 A; A/B=31-326.
DR PDB; 1OFY; X-ray; 2.00 A; A/B=31-326.
DR PDBsum; 19HC; -.
DR PDBsum; 1OFW; -.
DR PDBsum; 1OFY; -.
DR AlphaFoldDB; Q9RN68; -.
DR SMR; Q9RN68; -.
DR STRING; 525146.Ddes_2038; -.
DR DrugBank; DB03317; Ferroheme C.
DR EnsemblBacteria; ACL49934; ACL49934; Ddes_2038.
DR KEGG; dds:Ddes_2038; -.
DR eggNOG; COG0484; Bacteria.
DR HOGENOM; CLU_851850_0_0_7; -.
DR OrthoDB; 738283at2; -.
DR EvolutionaryTrace; Q9RN68; -.
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 InterPro; IPR002322; Cyt_c_III.
DR InterPro; IPR020942; Cyt_c_III_dom.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR Pfam; PF02085; Cytochrom_CIII; 2.
DR PRINTS; PR00609; CYTOCHROMEC3.
DR SUPFAM; SSF48695; SSF48695; 1.
DR PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Heme; Iron; Metal-binding; Periplasm;
KW Repeat; Signal; Transport.
FT SIGNAL 1..30
FT CHAIN 31..326
FT /note="Nine-heme cytochrome c"
FT /id="PRO_0000006594"
FT BINDING 67
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 70
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 77
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT BINDING 80
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT BINDING 81
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 82
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 89
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT BINDING 92
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT BINDING 93
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 111
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 127
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT BINDING 130
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT BINDING 131
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 141
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT BINDING 144
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT BINDING 145
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 157
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /note="covalent"
FT BINDING 160
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /note="covalent"
FT BINDING 161
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 227
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="6"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 230
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="8"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 248
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 255
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="6"
FT /note="covalent"
FT BINDING 258
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="6"
FT /note="covalent"
FT BINDING 259
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="6"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 260
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="7"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 271
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="7"
FT /note="covalent"
FT BINDING 274
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="7"
FT /note="covalent"
FT BINDING 275
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="7"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 294
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="9"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 297
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="8"
FT /note="covalent"
FT BINDING 300
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="8"
FT /note="covalent"
FT BINDING 301
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="8"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 314
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="9"
FT /note="covalent"
FT BINDING 317
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="9"
FT /note="covalent"
FT BINDING 318
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="9"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:1OFW"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:1OFW"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:1OFW"
FT HELIX 67..73
FT /evidence="ECO:0007829|PDB:1OFW"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:1OFW"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:1OFW"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:1OFW"
FT HELIX 106..111
FT /evidence="ECO:0007829|PDB:1OFW"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1OFW"
FT HELIX 127..137
FT /evidence="ECO:0007829|PDB:1OFW"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:1OFW"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:1OFW"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:1OFW"
FT HELIX 169..177
FT /evidence="ECO:0007829|PDB:1OFW"
FT HELIX 182..194
FT /evidence="ECO:0007829|PDB:1OFW"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:1OFW"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:1OFW"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:1OFW"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:1OFW"
FT HELIX 227..236
FT /evidence="ECO:0007829|PDB:1OFW"
FT TURN 237..240
FT /evidence="ECO:0007829|PDB:1OFW"
FT HELIX 242..247
FT /evidence="ECO:0007829|PDB:1OFW"
FT HELIX 253..257
FT /evidence="ECO:0007829|PDB:1OFW"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:1OFW"
FT HELIX 289..303
FT /evidence="ECO:0007829|PDB:1OFW"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:1OFW"
SQ SEQUENCE 326 AA; 35025 MW; 2ED7025ADDF250E3 CRC64;
MRNGTSLLLL AAIALAGAAC LTAMGGTAKA AALEPTDSGA PSAIVMFPVG EKPNPKGAAM
KPVVFNHLIH EKKIDNCETC HHTGDPVSCS TCHTVEGKAE GNYITLDRAM HATNIAKRAK
GNTPVSCVSC HEQQTKERRE CAGCHAIVTP KRDEAWCATC HNITPSMTPE QMQKGINGTL
LPGDNEALAA ETVLAQKTVE PVSPMLAPYK VVIDALADKY EPSNFTHRRH LTSLMERIKD
DKLAQAFHNK PEILCATCHH RSPLSLTPPK CGSCHTKEID KANPGRPNLM AAYHLQCMGC
HKGMDVARPR DTDCTTCHKA APKSAD
