PHEB_AGACH
ID PHEB_AGACH Reviewed; 177 AA.
AC Q7SIF9;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=R-phycoerythrin beta chain;
GN Name=rpeB;
OS Agarophyton chilensis (Red alga) (Gracilaria chilensis).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gracilariales;
OC Gracilariaceae; Agarophyton.
OX NCBI_TaxID=2510777;
RN [1] {ECO:0000305, ECO:0000312|PDB:1EYX}
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH PHYCOERYTHROBILIN;
RP PHYCOUROBILIN AND PHEA, FUNCTION, SUBUNIT, AND METHYLATION AT ASN-72.
RX PubMed=11134927; DOI=10.1107/s0907444900015274;
RA Contreras-Martel C., Martinez-Oyanedel J., Bunster M., Legrand P.,
RA Piras C., Vernede X., Fontecilla-Camps J.-C.;
RT "Crystallization and 2.2 A resolution structure of R-phycoerythrin from
RT Gracilaria chilensis: a case of perfect hemihedral twinning.";
RL Acta Crystallogr. D 57:52-60(2001).
CC -!- FUNCTION: Light-harvesting photosynthetic tetrapyrrole chromophore-
CC protein from the phycobiliprotein complex.
CC {ECO:0000269|PubMed:11134927}.
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:0000250|UniProtKB:Q01922, ECO:0000269|PubMed:11134927}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane;
CC Peripheral membrane protein; Stromal side. Note=Forms the periphery of
CC the phycobilisome rod.
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. {ECO:0000269|PubMed:11134927}.
CC -!- SIMILARITY: Belongs to the phycobiliprotein family. {ECO:0000255}.
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DR PDB; 1EYX; X-ray; 2.25 A; B/L=1-177.
DR PDBsum; 1EYX; -.
DR AlphaFoldDB; Q7SIF9; -.
DR SMR; Q7SIF9; -.
DR iPTMnet; Q7SIF9; -.
DR EvolutionaryTrace; Q7SIF9; -.
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_0000239448"
FT BINDING 35
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11134927"
FT BINDING 39
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11134927"
FT BINDING 50
FT /ligand="phycourobilin"
FT /ligand_id="ChEBI:CHEBI:189062"
FT /note="covalent, via 2 links"
FT /evidence="ECO:0000269|PubMed:11134927"
FT BINDING 54
FT /ligand="phycourobilin"
FT /ligand_id="ChEBI:CHEBI:189062"
FT /evidence="ECO:0000269|PubMed:11134927"
FT BINDING 61
FT /ligand="phycourobilin"
FT /ligand_id="ChEBI:CHEBI:189062"
FT /note="covalent, via 2 links"
FT /evidence="ECO:0000269|PubMed:11134927"
FT BINDING 72
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11134927"
FT BINDING 77..78
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11134927"
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:11134927"
FT BINDING 84..85
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11134927"
FT BINDING 147..148
FT /ligand="phycourobilin"
FT /ligand_id="ChEBI:CHEBI:189062"
FT /evidence="ECO:0000269|PubMed:11134927"
FT BINDING 154
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11134927"
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:11134927"
FT MOD_RES 72
FT /note="N4-methylasparagine"
FT /evidence="ECO:0000269|PubMed:11134927"
FT HELIX 6..13
FT /evidence="ECO:0007829|PDB:1EYX"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:1EYX"
FT HELIX 21..32
FT /evidence="ECO:0007829|PDB:1EYX"
FT HELIX 34..45
FT /evidence="ECO:0007829|PDB:1EYX"
FT HELIX 48..61
FT /evidence="ECO:0007829|PDB:1EYX"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:1EYX"
FT HELIX 76..99
FT /evidence="ECO:0007829|PDB:1EYX"
FT HELIX 103..108
FT /evidence="ECO:0007829|PDB:1EYX"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:1EYX"
FT HELIX 124..142
FT /evidence="ECO:0007829|PDB:1EYX"
FT HELIX 159..175
FT /evidence="ECO:0007829|PDB:1EYX"
SQ SEQUENCE 177 AA; 18604 MW; F852E861B04D7DA1 CRC64;
MLDAFSRVIS NADAKAAYVG GSDLQALRTF ISDGNKRLDA VNYIVSNSSC IVSDAISGMI
CENPGLITPG GNCYTNRRMA ACLRDGEIIL RYISYALLAG DSSVLEDRCL NGLKETYIAL
GVPTNSTVRA VSIMKAAVGA FISNTASQRK GEVIEGDCSA LAAEIASYCD RISAAVS
