PHCB_PORPP
ID PHCB_PORPP Reviewed; 172 AA.
AC P37208;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=R-phycocyanin-1 beta chain;
DE AltName: Full=R-phycocyanin I beta chain;
GN Name=rpcB; Synonyms=cpcB;
OS Porphyridium purpureum (Red alga) (Porphyridium cruentum).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Porphyridiales; Porphyridiaceae;
OC Porphyridium.
OX NCBI_TaxID=35688;
RN [1]
RP PROTEIN SEQUENCE, SUBUNIT, SUBCELLULAR LOCATION, CHROMOPHORES, AND
RP METHYLATION AT ASN-72.
RC STRAIN=1380-1A;
RX PubMed=8168545; DOI=10.1111/j.1432-1033.1994.tb18769.x;
RA Ducret A., Sidler W., Frank G., Zuber H.;
RT "The complete amino acid sequence of R-phycocyanin-I alpha and beta
RT subunits from the red alga Porphyridium cruentum. Structural and
RT phylogenetic relationships of the phycocyanins within the phycobiliprotein
RT families.";
RL Eur. J. Biochem. 221:563-580(1994).
CC -!- FUNCTION: Light-harvesting photosynthetic bile pigment-protein from the
CC phycobiliprotein complex (phycobilisome, PBS). Phycocyanin is the major
CC phycobiliprotein in the PBS rod.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain (PubMed:8168545).
CC Dimers further assemble into trimers and the trimers into hexamers. The
CC basic functional unit of phycobiliproteins is a ring-shaped hexamer
CC formed from two back-to-back trimers contacting via the alpha chain
CC subunits. The trimers are composed of alpha/beta subunit heterodimers
CC arranged around a three-fold axis of symmetry. The phycoerythrins also
CC contain a gamma subunit which is located in the center of the hexamer
CC (By similarity). {ECO:0000250|UniProtKB:P00311,
CC ECO:0000269|PubMed:8168545}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane;
CC Peripheral membrane protein; Stromal side. Note=Part of the
CC phycobilisome rod. {ECO:0000269|PubMed:8168545}.
CC -!- PTM: Contains two covalently linked bilin chromophores.
CC {ECO:0000269|PubMed:8168545}.
CC -!- SIMILARITY: Belongs to the phycobiliprotein family. {ECO:0000305}.
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DR PIR; S43239; S43239.
DR AlphaFoldDB; P37208; -.
DR SMR; P37208; -.
DR iPTMnet; P37208; -.
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 Antenna complex; Bile pigment; Chloroplast; Chromophore;
KW Direct protein sequencing; Electron transport; Membrane; Methylation;
KW Photosynthesis; Phycobilisome; Plastid; Thylakoid; Transport.
FT CHAIN 1..172
FT /note="R-phycocyanin-1 beta chain"
FT /id="PRO_0000199163"
FT BINDING 82
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000250|UniProtKB:P59859,
FT ECO:0000305|PubMed:8168545"
FT BINDING 153
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000250|UniProtKB:P59859,
FT ECO:0000305|PubMed:8168545"
FT MOD_RES 72
FT /note="N4-methylasparagine"
FT /evidence="ECO:0000269|PubMed:8168545"
SQ SEQUENCE 172 AA; 18171 MW; F90C62FD4AEA7227 CRC64;
MLDAFAKVVA QADARGEFLS NTQIDALSKM VKEGNQRLDI VNKVTSNASA IVTNSARALF
AEQPQLIQPG GNAYTSRNMA ACLRDMEIVL RYVSYAMLAG DSSVLDDRCL NGLRETYQAL
GTPGSSVAVA IQKMKDASVA LANDTTGTPI GDCSSLVAEL AGYFDRAAVS VV