CYCR_ROSDO
ID CYCR_ROSDO Reviewed; 371 AA.
AC P26278; Q16DV6; Q52727;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Photosynthetic reaction center cytochrome c subunit;
GN Name=pufC; Synonyms=cytC; OrderedLocusNames=RD1_0102;
OS Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS (strain OCh 114)) (Roseobacter denitrificans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=375451;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9286973; DOI=10.1128/jb.179.17.5247-5258.1997;
RA Kortluke C., Breese K., Gad'on N., Labahn A., Drews G.;
RT "Structure of the puf operon of the obligately aerobic, bacteriochlorophyll
RT alpha-containing bacterium Roseobacter denitrificans OCh114 and its
RT expression in a Rhodobacter capsulatus puf puc deletion mutant.";
RL J. Bacteriol. 179:5247-5258(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33942 / OCh 114;
RX PubMed=17098896; DOI=10.1128/jb.01390-06;
RA Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA Touchman J.W.;
RT "The complete genome sequence of Roseobacter denitrificans reveals a
RT mixotrophic rather than photosynthetic metabolism.";
RL J. Bacteriol. 189:683-690(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-187.
RX PubMed=1787796; DOI=10.1111/j.1365-2958.1991.tb00792.x;
RA Liebetanz R., Hornberger U., Drews G.;
RT "Organization of the genes coding for the reaction-centre L and M subunits
RT and B870 antenna polypeptides alpha and beta from the aerobic
RT photosynthetic bacterium Erythrobacter species OCH114.";
RL Mol. Microbiol. 5:1459-1468(1991).
CC -!- FUNCTION: The reaction center of purple bacteria contains a tightly
CC bound cytochrome molecule which re-reduces the photo oxidized primary
CC electron donor. {ECO:0000250|UniProtKB:P07173}.
CC -!- SUBUNIT: Component of the photosynthetic reaction center composed of
CC protein subunits L (PufL), M (PufM), H (PuhA) and cytochrome C (PufC).
CC The reaction center interacts with light-harvesting antenna complex
CC LH1. {ECO:0000250|UniProtKB:D2Z0P5}.
CC -!- SUBCELLULAR LOCATION: Cellular chromatophore membrane
CC {ECO:0000250|UniProtKB:P07173}.
CC -!- PTM: Binds 4 heme groups per subunit. {ECO:0000250|UniProtKB:P07173}.
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DR EMBL; X83392; CAA58310.1; -; Genomic_DNA.
DR EMBL; CP000362; ABG29837.1; -; Genomic_DNA.
DR EMBL; X57597; CAA40820.1; -; Genomic_DNA.
DR PIR; S16314; S16314.
DR RefSeq; WP_011566459.1; NZ_FOOO01000011.1.
DR AlphaFoldDB; P26278; -.
DR SMR; P26278; -.
DR STRING; 375451.RD1_0102; -.
DR EnsemblBacteria; ABG29837; ABG29837; RD1_0102.
DR KEGG; rde:RD1_0102; -.
DR eggNOG; ENOG502Z7SF; Bacteria.
DR HOGENOM; CLU_050380_0_0_5; -.
DR OMA; CTYCHNT; -.
DR OrthoDB; 374575at2; -.
DR Proteomes; UP000007029; Chromosome.
DR GO; GO:0030077; C:plasma membrane light-harvesting complex; IEA:InterPro.
DR GO; GO:0042717; C:plasma membrane-derived chromatophore membrane; 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:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0019684; P:photosynthesis, light reaction; IEA:InterPro.
DR CDD; cd09224; CytoC_RC; 1.
DR Gene3D; 1.10.468.10; -; 2.
DR InterPro; IPR023119; Multihaem_cyt_PRC_cyt_su-like.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR InterPro; IPR003158; Photosyn_RC_cyt_c-su.
DR Pfam; PF02276; CytoC_RC; 1.
DR PIRSF; PIRSF000017; RC_cytochrome; 1.
DR SUPFAM; SSF48695; SSF48695; 1.
DR PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE 3: Inferred from homology;
KW Electron transport; Heme; Iron; Membrane; Metal-binding; Photosynthesis;
KW Reaction center; Reference proteome; Repeat; Transport.
FT CHAIN 1..371
FT /note="Photosynthetic reaction center cytochrome c subunit"
FT /id="PRO_0000108413"
FT BINDING 114
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|UniProtKB:P07173"
FT BINDING 127
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07173"
FT BINDING 130
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07173"
FT BINDING 131
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|UniProtKB:P07173"
FT BINDING 153
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|UniProtKB:P07173"
FT BINDING 167
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 /evidence="ECO:0000250|UniProtKB:P07173"
FT BINDING 178
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07173"
FT BINDING 181
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07173"
FT BINDING 182
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|UniProtKB:P07173"
FT BINDING 267
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|UniProtKB:P07173"
FT BINDING 278
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07173"
FT BINDING 281
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07173"
FT BINDING 282
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|UniProtKB:P07173"
FT BINDING 339
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07173"
FT BINDING 342
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07173"
FT BINDING 343
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 /evidence="ECO:0000250|UniProtKB:P07173"
FT CONFLICT 236
FT /note="V -> G (in Ref. 1; CAA58310)"
FT /evidence="ECO:0000305"
FT CONFLICT 348..371
FT /note="KPMQGLNVIADWPELATTEAPVYE -> NRCKA (in Ref. 1;
FT CAA58310)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 371 AA; 41168 MW; ADE844C1AA6E91C8 CRC64;
MFPKWFDKWN ADNPTNIFGP AILIGVLGVA VFGAAAIVSI GNPAQTASMQ TGPRGTGMHV
AEFNVTRFAP DPTIEEYYTE APYIPEGGEE LAKDIYENVQ VLGDLTDDNF NRVMTAMTQW
IAPEEGCVYC HGEGDLETYG EDNLYTKVVA RRMIQMTQNI NENWDGHVNA NAEVGVNCYT
CHRGEHVPSE IWFNITPVTE ATAGWASVQN RATPLSQSTS LPSNALEIYL TEYEAVNVHD
LESRVAGVPN DVEVASIQKT EMTFSLMNYF SNSLGVNCVF CHNSRAFYDP GQHTPQWATA
LLGRQMVIEM NQEYLIPLED EYPEDRLGPV YADAPKAACK TCHKGYQKPM QGLNVIADWP
ELATTEAPVY E
