CYC7_GEOMG
ID CYC7_GEOMG Reviewed; 90 AA.
AC P81894; Q39RK4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Cytochrome c7;
DE Flags: Precursor;
GN OrderedLocusNames=Gmet_2902;
OS Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=269799;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53774 / DSM 7210 / GS-15;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Geobacter metallireducens GS-15.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 21-37, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10386369; DOI=10.1111/j.1574-6968.1999.tb13621.x;
RA Afkar E., Fukumori Y.;
RT "Purification and characterization of triheme cytochrome c7 from the metal-
RT reducing bacterium, Geobacter metallireducens.";
RL FEMS Microbiol. Lett. 175:205-210(1999).
RN [3]
RP PROTEIN SEQUENCE OF 21-57, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MASS SPECTROMETRY.
RX DOI=10.1006/anae.2000.0333;
RA Champine J.E., Underhill B., Johnston J.M., Lilly W.W., Goodwin S.;
RT "Electron transfer in the dissimilatory iron-reducing bacterium Geobacter
RT metallireducens.";
RL Anaerobe 6:187-196(2000).
CC -!- FUNCTION: May be involved in anaerobic iron respiration.
CC {ECO:0000269|PubMed:10386369, ECO:0000269|Ref.3}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is -91 mV (Ref.3) or -190 mV. {ECO:0000269|PubMed:10386369,
CC ECO:0000269|Ref.3};
CC -!- PTM: Binds 3 heme groups per subunit.
CC -!- MASS SPECTROMETRY: Mass=9684; Mass_error=10; Method=MALDI;
CC Evidence={ECO:0000269|Ref.3};
CC -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
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DR EMBL; CP000148; ABB33120.1; -; Genomic_DNA.
DR RefSeq; WP_004512838.1; NC_007517.1.
DR AlphaFoldDB; P81894; -.
DR SMR; P81894; -.
DR STRING; 269799.Gmet_2902; -.
DR EnsemblBacteria; ABB33120; ABB33120; Gmet_2902.
DR KEGG; gme:Gmet_2902; -.
DR eggNOG; ENOG50335B9; Bacteria.
DR HOGENOM; CLU_188310_0_0_7; -.
DR OMA; HSAKNEC; -.
DR OrthoDB; 738283at2; -.
DR Proteomes; UP000007073; Chromosome.
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.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW Reference proteome; Signal; Sulfate respiration; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:10386369, ECO:0000269|Ref.3"
FT CHAIN 21..90
FT /note="Cytochrome c7"
FT /id="PRO_0000108368"
FT BINDING 37
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 /evidence="ECO:0000250"
FT BINDING 40
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 /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 51
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 /evidence="ECO:0000250"
FT BINDING 67
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 /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 74
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 /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 88
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 /evidence="ECO:0000250"
FT CONFLICT 22..23
FT /note="DE -> RR (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="H -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="C -> K (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 90 AA; 9898 MW; E313736D14B27DFF CRC64;
MKRIIASLAL SVFCAGLAFA ADELTFKAKN GDVKFPHKKH QQVVGNCKKC HEKGPGKIEG
FGKDWAHKTC KGCHEEMKKG PTKCGDCHKK
