PHCB_CYACA
ID PHCB_CYACA Reviewed; 172 AA.
AC O19909;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=C-phycocyanin beta chain;
GN Name=cpcB;
OS Cyanidium caldarium (Red alga).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Cyanidium.
OX NCBI_TaxID=2771;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RK-1;
RX PubMed=11040290; DOI=10.1007/s002390010101;
RA Gloeckner G., Rosenthal A., Valentin K.-U.;
RT "The structure and gene repertoire of an ancient red algal plastid
RT genome.";
RL J. Mol. Evol. 51:382-390(2000).
CC -!- FUNCTION: Light-harvesting photosynthetic tetrapyrrole chromophore-
CC protein from the phycobiliprotein complex (phycobilisome, PBS).
CC Phycocyanin is the major phycobiliprotein in the PBS rod.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit, which further
CC assembles into trimers and the trimers into hexamers. The basic
CC functional unit of phycobiliproteins is a ring-shaped hexamer formed
CC from two back-to-back trimers contacting via the alpha chain subunits.
CC The trimers are composed of alpha/beta subunit heterodimers arranged
CC around a three-fold axis of symmetry. The phycoerythrins also contain a
CC gamma subunit which is located in the center of the hexamer.
CC {ECO:0000250|UniProtKB:P00311}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Stromal side
CC {ECO:0000250}. Note=Part of the phycobilisome rod. {ECO:0000250}.
CC -!- PTM: Contains two covalently linked phycocyanobilin chromophores.
CC {ECO:0000250|UniProtKB:P00311}.
CC -!- MISCELLANEOUS: The light-harvesting antenna system in red algae and
CC cyanobacteria is formed of phycobilisomes. These are composed of the
CC phycobiliproteins phycoerythrin (CPE), phycocyanin (CPC) and
CC allophycocyanin (APC). Cyanobacteria also contain phycoerythrocyanin
CC (PCC). The phycobiliproteins all share the same subunit composition and
CC organization with variations in the covalently bound open-chain
CC tetrapyrrole chromophores. The phycobiliprotein complexes are arranged
CC sequentially in antenna complexes linked by linker proteins with CPE at
CC the periphery, CPC in the middle and APC at the core feeding to the
CC photosynthetic reaction center.
CC -!- SIMILARITY: Belongs to the phycobiliprotein family. {ECO:0000305}.
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DR EMBL; AF022186; AAB82680.1; -; Genomic_DNA.
DR PIR; T11977; T11977.
DR RefSeq; NP_045081.1; NC_001840.1.
DR PDB; 6Y3D; X-ray; 1.80 A; BBB/DDD/FFF/HHH/JJJ/LLL=1-172.
DR PDBsum; 6Y3D; -.
DR AlphaFoldDB; O19909; -.
DR SMR; O19909; -.
DR GeneID; 800251; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030089; C:phycobilisome; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.490.20; -; 1.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012128; Phycobilisome_asu/bsu.
DR InterPro; IPR038719; Phycobilisome_asu/bsu_sf.
DR InterPro; IPR006247; Phycocyanin_b.
DR Pfam; PF00502; Phycobilisome; 1.
DR PIRSF; PIRSF000081; Phycocyanin; 1.
DR SUPFAM; SSF46458; SSF46458; 1.
DR TIGRFAMs; TIGR01339; phycocy_beta; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antenna complex; Bile pigment; Chloroplast; Chromophore;
KW Electron transport; Membrane; Methylation; Photosynthesis; Phycobilisome;
KW Plastid; Thylakoid; Transport.
FT CHAIN 1..172
FT /note="C-phycocyanin beta chain"
FT /id="PRO_0000199148"
FT BINDING 35
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 82..88
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="2"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000250|UniProtKB:P00311"
FT BINDING 149..151
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="1"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000250|UniProtKB:P00311"
FT MOD_RES 72
FT /note="N4-methylasparagine"
FT /evidence="ECO:0000250|UniProtKB:P00311"
SQ SEQUENCE 172 AA; 18174 MW; 72622C72CFB841CD CRC64;
MLDAFSKVVA QADARGEFLS NTQLDALSKM VADGNKRLDA TAAISANAAT IVTNAARSLF
SEQPQLIQPG GNAYTNRRMA ACLRDMEIIL RYVSYATIAG DSSVLDDRCL NGLRETYQAL
GVPGASVALA VEKMKEAAIA FANDSSNVTI GDCSALISEI ATYFDRAAKA VV
