CYCR_ALLVD
ID CYCR_ALLVD Reviewed; 383 AA.
AC O82947; D3RP71;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Photosynthetic reaction center cytochrome c subunit;
DE Flags: Precursor;
GN Name=pufC; OrderedLocusNames=Alvin_2551;
OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS 10441 / D) (Chromatium vinosum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=572477;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Corson G.E., Nagashima K.V., Matsuura K., Sakuragi Y., Ruwanthi W., Qin H.,
RA Allen R., Knaff D.B.;
RT "Primary structure of genes encoding light-harvesting and reaction center
RT proteins from Chromatium vinosum.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX PubMed=22675582; DOI=10.4056/sigs.2335270;
RA Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL Stand. Genomic Sci. 5:311-330(2011).
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:D2Z0P5}; Lipid-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00303}.
CC -!- PTM: Binds 4 heme groups per subunit. {ECO:0000250|UniProtKB:P07173}.
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DR EMBL; AB011811; BAA32742.1; -; Genomic_DNA.
DR EMBL; CP001896; ADC63461.1; -; Genomic_DNA.
DR RefSeq; WP_012971730.1; NC_013851.1.
DR AlphaFoldDB; O82947; -.
DR SMR; O82947; -.
DR STRING; 572477.Alvin_2551; -.
DR EnsemblBacteria; ADC63461; ADC63461; Alvin_2551.
DR KEGG; alv:Alvin_2551; -.
DR eggNOG; ENOG502Z7SF; Bacteria.
DR HOGENOM; CLU_050380_0_0_6; -.
DR OMA; CTYCHNT; -.
DR OrthoDB; 374575at2; -.
DR Proteomes; UP000001441; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Electron transport; Heme; Iron; Lipoprotein; Membrane; Metal-binding;
KW Palmitate; Photosynthesis; Reaction center; Reference proteome; Repeat;
KW Signal; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 23..383
FT /note="Photosynthetic reaction center cytochrome c subunit"
FT /id="PRO_0000006549"
FT REGION 335..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 94
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 107
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07173"
FT BINDING 110
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07173"
FT BINDING 111
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 130
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 144
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 152
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07173"
FT BINDING 155
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07173"
FT BINDING 156
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 236
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 247
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07173"
FT BINDING 250
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07173"
FT BINDING 251
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 307
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07173"
FT BINDING 310
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P07173"
FT BINDING 311
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 LIPID 23
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 23
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CONFLICT 13
FT /note="A -> D (in Ref. 1; BAA32742)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 383 AA; 41479 MW; 959DD9E59FD4190E CRC64;
MNLGKQLTLP AVAVVASVVL LGCERPPPEV VQKGYRGVAM EQNYNPRLLE ASIKANLPVE
SLPAAAPGGP SVSDVYENVQ VLKDLSVAEF TRTMVAVTTW VAPKEGCNYC HVPGNWASDD
IYTKVVSRRM FELVRATNSN WKDHVAETGV TCYTCHRGNP VPKYVWVTDP GPNQPSGVTP
TGQNYASSTV AYSALPLDPY TPFLDQSNEI RVIGQTALPA GNTTSLKQAE WTYGLMMQIS
DSLGVNCTFC HNSRSFYDWK QSTPQRTTAW YAIRHVRDIN QNYIWPLNDA LPASRKGPYG
DPFKVGCMTC HQGAYKPLYG AQMAKDYPAL YESAPAEAAP ATEEAPAAEA EAVEAAPVEE
AAPAPVEQAA APVEDAAPAP QQL
