PHEB_GRIMO
ID PHEB_GRIMO Reviewed; 177 AA.
AC O36004;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=R-phycoerythrin beta chain;
GN Name=cpeB;
OS Griffithsia monilis (Red alga).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Ceramiales;
OC Ceramiaceae; Griffithsia.
OX NCBI_TaxID=42003;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN
RP COMPLEX WITH PHYCOERYTHROBILIN; PHYCOUROBILIN AND CPEA, SUBUNIT, AND
RP METHYLATION AT ASN-72.
RX PubMed=10388620; DOI=10.1006/jsbi.1999.4106;
RA Ritter S., Hiller R.G., Wrench P.M., Welte W., Diederichs K.;
RT "Crystal structure of a phycourobilin-containing phycoerythrin at 1.90-A
RT resolution.";
RL J. Struct. Biol. 126:86-97(1999).
CC -!- FUNCTION: Light-harvesting photosynthetic tetrapyrrole chromophore-
CC protein from the phycobiliprotein complex.
CC -!- SUBUNIT: Heterododecamer of 6 alpha and 6 beta chains. 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:0000269|PubMed:10388620}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Stromal side
CC {ECO:0000250}. Note=Forms the periphery of the phycobilisome rod.
CC {ECO:0000250}.
CC -!- PTM: Contains two covalently linked phycoerythrobilin chromophores and
CC one covalently linked phycourobilin chromophore.
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; Z98528; CAB11028.1; -; Genomic_DNA.
DR PDB; 1B8D; X-ray; 1.90 A; B/L=1-177.
DR PDBsum; 1B8D; -.
DR AlphaFoldDB; O36004; -.
DR SMR; O36004; -.
DR iPTMnet; O36004; -.
DR PRIDE; O36004; -.
DR EvolutionaryTrace; O36004; -.
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 Pfam; PF00502; Phycobilisome; 1.
DR PIRSF; PIRSF000081; Phycocyanin; 1.
DR SUPFAM; SSF46458; SSF46458; 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..177
FT /note="R-phycoerythrin beta chain"
FT /id="PRO_0000199191"
FT BINDING 35
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10388620"
FT BINDING 39
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10388620"
FT BINDING 50
FT /ligand="phycourobilin"
FT /ligand_id="ChEBI:CHEBI:189062"
FT /note="covalent, via 2 links"
FT /evidence="ECO:0000269|PubMed:10388620"
FT BINDING 54
FT /ligand="phycourobilin"
FT /ligand_id="ChEBI:CHEBI:189062"
FT /evidence="ECO:0000269|PubMed:10388620"
FT BINDING 61
FT /ligand="phycourobilin"
FT /ligand_id="ChEBI:CHEBI:189062"
FT /note="covalent, via 2 links"
FT /evidence="ECO:0000269|PubMed:10388620"
FT BINDING 72
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10388620"
FT BINDING 77..78
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="1"
FT BINDING 82
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="1"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000269|PubMed:10388620"
FT BINDING 84..85
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="1"
FT BINDING 147..148
FT /ligand="phycourobilin"
FT /ligand_id="ChEBI:CHEBI:189062"
FT BINDING 158
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="2"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000269|PubMed:10388620"
FT MOD_RES 72
FT /note="N4-methylasparagine"
FT /evidence="ECO:0000269|PubMed:10388620"
FT HELIX 4..13
FT /evidence="ECO:0007829|PDB:1B8D"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:1B8D"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:1B8D"
FT HELIX 34..46
FT /evidence="ECO:0007829|PDB:1B8D"
FT HELIX 48..62
FT /evidence="ECO:0007829|PDB:1B8D"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:1B8D"
FT HELIX 76..99
FT /evidence="ECO:0007829|PDB:1B8D"
FT HELIX 103..108
FT /evidence="ECO:0007829|PDB:1B8D"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:1B8D"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:1B8D"
FT HELIX 124..142
FT /evidence="ECO:0007829|PDB:1B8D"
FT HELIX 159..176
FT /evidence="ECO:0007829|PDB:1B8D"
SQ SEQUENCE 177 AA; 18482 MW; 73B87ACD8A165B52 CRC64;
MLDAFSRVVV TSDAKAAYVG GSDLQSLKSF INDGNKRLDA VNYIVSNASC IVSDAVSGMI
CENPGLIAPG GNCYTNRRMA ACLRDGEIIL RYVSYALLAG DSSVLDDRCL NGLKETYIAL
GVPTASSSRA VSIMKATATA FITNTASGRK VEVAAGDCQA LQAEAASYFD KVGSSID
