ID Q74G83_GEOSL Unreviewed; 91 AA.
AC Q74G83;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Cytochrome c {ECO:0000313|EMBL:AAR33696.1};
GN Name=ppcB {ECO:0000313|EMBL:AAR33696.1};
GN OrderedLocusNames=GSU0364 {ECO:0000313|EMBL:AAR33696.1};
OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=243231 {ECO:0000313|EMBL:AAR33696.1, ECO:0000313|Proteomes:UP000000577};
RN [1] {ECO:0000313|EMBL:AAR33696.1, ECO:0000313|Proteomes:UP000000577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51573 / DSM 12127 / PCA
RC {ECO:0000313|Proteomes:UP000000577};
RX PubMed=14671304; DOI=10.1126/science.1088727;
RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.,
RA Heidelberg J.F., Wu D., Wu M., Ward N., Beanan M.J., Dodson R.J.,
RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn M.,
RA Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J., Davidsen T.M.,
RA Zafar N., White O., Tran B., Romero C., Forberger H.A., Weidman J.,
RA Khouri H., Feldblyum T.V., Utterback T.R., Van Aken S.E., Lovley D.R.,
RA Fraser C.M.;
RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT environments.";
RL Science 302:1967-1969(2003).
RN [2] {ECO:0007829|PDB:3BXU}
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 21-91 IN COMPLEX WITH HEME B.
RX PubMed=18534185; DOI=10.1016/j.bbabio.2008.04.043;
RA Morgado L., Bruix M., Orshonsky V., Londer Y.Y., Duke N.E., Yang X.,
RA Pokkuluri P.R., Schiffer M., Salgueiro C.A.;
RT "Structural insights into the modulation of the redox properties of two
RT Geobacter sulfurreducens homologous triheme cytochromes.";
RL Biochim. Biophys. Acta 1777:1157-1165(2008).
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000256|PIRSR:PIRSR602322-1};
CC Note=Binds 4 heme c groups covalently per monomer.
CC {ECO:0000256|PIRSR:PIRSR602322-1};
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DR EMBL; AE017180; AAR33696.1; -; Genomic_DNA.
DR RefSeq; NP_951423.1; NC_002939.5.
DR RefSeq; WP_010941032.1; NC_002939.5.
DR PDB; 3BXU; X-ray; 1.35 A; A/B=21-91.
DR PDBsum; 3BXU; -.
DR AlphaFoldDB; Q74G83; -.
DR SMR; Q74G83; -.
DR STRING; 243231.GSU0364; -.
DR EnsemblBacteria; AAR33696; AAR33696; GSU0364.
DR KEGG; gsu:GSU0364; -.
DR PATRIC; fig|243231.5.peg.362; -.
DR eggNOG; ENOG50335B9; Bacteria.
DR HOGENOM; CLU_188310_0_0_7; -.
DR InParanoid; Q74G83; -.
DR OrthoDB; 5421852at2; -.
DR EvolutionaryTrace; Q74G83; -.
DR Proteomes; UP000000577; 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 CDD; cd08168; Cytochrom_C3; 1.
DR Gene3D; 3.90.10.10; Cytochrome C3; 1.
DR InterPro; IPR029467; Cyt_c7-like.
DR InterPro; IPR002322; Cyt_c_III.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR Pfam; PF14522; Cytochrome_C7; 1.
DR PRINTS; PR00609; CYTOCHROMEC3.
DR SUPFAM; SSF48695; Multiheme cytochromes; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:3BXU};
KW Heme {ECO:0000256|PIRSR:PIRSR602322-1, ECO:0007829|PDB:3BXU};
KW Iron {ECO:0000256|PIRSR:PIRSR602322-1, ECO:0007829|PDB:3BXU};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR602322-1, ECO:0007829|PDB:3BXU};
KW Reference proteome {ECO:0000313|Proteomes:UP000000577};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..91
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004285402"
FT DOMAIN 33..90
FT /note="Cytochrome c7-like"
FT /evidence="ECO:0000259|Pfam:PF14522"
FT BINDING 27
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:3BXU"
FT BINDING 29
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:3BXU"
FT BINDING 37
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /ligand_part_note="axial binding residue"
FT /evidence="ECO:0007829|PDB:3BXU"
FT BINDING 37
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:0000256|PIRSR:PIRSR602322-1"
FT BINDING 39
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="3"
FT /evidence="ECO:0007829|PDB:3BXU"
FT BINDING 40
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /ligand_part_note="axial binding residue"
FT /evidence="ECO:0007829|PDB:3BXU"
FT BINDING 40
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:0000256|PIRSR:PIRSR602322-1"
FT BINDING 47
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:0000256|PIRSR:PIRSR602322-1"
FT BINDING 50
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:0000256|PIRSR:PIRSR602322-1"
FT BINDING 51
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /ligand_part_note="axial binding residue"
FT /evidence="ECO:0007829|PDB:3BXU"
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:0000256|PIRSR:PIRSR602322-1"
FT BINDING 57
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:3BXU"
FT BINDING 58
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:3BXU"
FT BINDING 67
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /ligand_part_note="axial binding residue"
FT /evidence="ECO:0007829|PDB:3BXU"
FT BINDING 71
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:0000256|PIRSR:PIRSR602322-1"
FT BINDING 74
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:0000256|PIRSR:PIRSR602322-1"
FT BINDING 75
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /ligand_part_note="axial binding residue"
FT /evidence="ECO:0007829|PDB:3BXU"
FT BINDING 75
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:0000256|PIRSR:PIRSR602322-1"
FT BINDING 85
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:0000256|PIRSR:PIRSR602322-1"
FT BINDING 88
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:0000256|PIRSR:PIRSR602322-1"
FT BINDING 89
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /ligand_part_note="axial binding residue"
FT /evidence="ECO:0007829|PDB:3BXU"
FT BINDING 89
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:0000256|PIRSR:PIRSR602322-1"
SQ SEQUENCE 91 AA; 9672 MW; 89A955A007DBB929 CRC64;
MKKLIASLAL TLFAAGAALA ADTMTFTAKN GNVTFDHKKH QTIVPDCAVC HGKTPGKIEG
FGKEMAHGKS CKGCHEEMKK GPTKCGECHK K
//
