PHEA_AGACH
ID PHEA_AGACH Reviewed; 164 AA.
AC Q7SIG0;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=R-phycoerythrin alpha chain;
GN Name=rpeA;
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 AND PHEB, FUNCTION, AND SUBUNIT.
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: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.
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:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PDB; 1EYX; X-ray; 2.25 A; A/K=1-164.
DR PDBsum; 1EYX; -.
DR AlphaFoldDB; Q7SIG0; -.
DR SMR; Q7SIG0; -.
DR EvolutionaryTrace; Q7SIG0; -.
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; Photosynthesis; Phycobilisome; Plastid;
KW Thylakoid; Transport.
FT CHAIN 1..164
FT /note="R-phycoerythrin alpha chain"
FT /id="PRO_0000239447"
FT BINDING 47
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11134927"
FT BINDING 81
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
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11134927"
FT BINDING 88
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11134927"
FT BINDING 137
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11134927"
FT BINDING 139
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 BINDING 142
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11134927"
FT HELIX 4..13
FT /evidence="ECO:0007829|PDB:1EYX"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:1EYX"
FT HELIX 21..62
FT /evidence="ECO:0007829|PDB:1EYX"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:1EYX"
FT STRAND 71..75
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 TURN 109..112
FT /evidence="ECO:0007829|PDB:1EYX"
FT HELIX 113..119
FT /evidence="ECO:0007829|PDB:1EYX"
FT HELIX 124..137
FT /evidence="ECO:0007829|PDB:1EYX"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:1EYX"
FT HELIX 148..162
FT /evidence="ECO:0007829|PDB:1EYX"
SQ SEQUENCE 164 AA; 17752 MW; 44D6EB97745B0E36 CRC64;
MKSVITTVIS AADSAGRFPS SSDLESVQGN IQRASARLEA AEKLASNHEA VVKEAGDACF
GKYGYLKNPG EAGENQEKIN KCYRDIDHYM RLVNYSLVIG GTGPLDEWGI AGAREVYRTL
NLPTSAYIAA FAFTRDRLCG PRDMSAQAGV EYSTALDYII NSLS
