PHEA_PORPP
ID PHEA_PORPP Reviewed; 164 AA.
AC P11392;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=B-phycoerythrin alpha chain;
GN Name=cpeA;
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.
RX PubMed=2495805; DOI=10.1515/bchm3.1989.370.1.115;
RA Sidler W., Kumpf B., Suter F., Klotz A.V., Glazer A.N., Zuber H.;
RT "The complete amino-acid sequence of the alpha and beta subunits of B-
RT phycoerythrin from the rhodophytan alga Porphyridium cruentum.";
RL Biol. Chem. Hoppe-Seyler 370:115-124(1989).
RN [2]
RP PROTEIN SEQUENCE OF 79-84 AND 136-142, AND CHROMOPHORE BINDING AT CYS-82
RP AND CYS-139.
RX PubMed=6715353; DOI=10.1016/s0021-9258(18)91035-5;
RA Lundell D.J., Glazer A.N., DeLange R.J., Brown D.M.;
RT "Bilin attachment sites in the alpha and beta subunits of B-phycoerythrin.
RT Amino acid sequence studies.";
RL J. Biol. Chem. 259:5472-5480(1984).
CC -!- FUNCTION: Light-harvesting photosynthetic bile pigment-protein from the
CC phycobiliprotein complex.
CC -!- SUBUNIT: Heteromer of 6 alpha, 6 beta and one gamma chain.
CC {ECO:0000250}.
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 bilin chromophores.
CC -!- SIMILARITY: Belongs to the phycobiliprotein family. {ECO:0000305}.
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 PIR; S02817; S02817.
DR PDB; 3V57; X-ray; 1.70 A; A/C=1-164.
DR PDB; 3V58; X-ray; 1.85 A; A/C=1-164.
DR PDBsum; 3V57; -.
DR PDBsum; 3V58; -.
DR AlphaFoldDB; P11392; -.
DR SMR; P11392; -.
DR IntAct; P11392; 1.
DR MINT; P11392; -.
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 Direct protein sequencing; Electron transport; Membrane; Photosynthesis;
KW Phycobilisome; Plastid; Thylakoid; Transport.
FT CHAIN 1..164
FT /note="B-phycoerythrin alpha chain"
FT /id="PRO_0000199176"
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 BINDING 139
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="2"
FT /note="covalent, via 1 link"
FT HELIX 4..15
FT /evidence="ECO:0007829|PDB:3V57"
FT HELIX 21..62
FT /evidence="ECO:0007829|PDB:3V57"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:3V57"
FT HELIX 76..99
FT /evidence="ECO:0007829|PDB:3V57"
FT HELIX 103..108
FT /evidence="ECO:0007829|PDB:3V57"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:3V57"
FT HELIX 113..119
FT /evidence="ECO:0007829|PDB:3V57"
FT HELIX 124..137
FT /evidence="ECO:0007829|PDB:3V57"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:3V57"
FT HELIX 146..162
FT /evidence="ECO:0007829|PDB:3V57"
SQ SEQUENCE 164 AA; 17817 MW; A704CE21D52B8D7E CRC64;
MKSVITTVVS AADAAGRFPS NSDLESIQGN IQRSAARLEA AEKLAGNHEA VVKEAGDACF
AKYAYLKNPG EAGENQEKIN KCYRDVDHYM RLVNYDLVVG GTGPLDEWGI AGAREVYRTL
NLPTSAYVAS IAYTRDRLCV PRDMSAQAGV EFSAYLDYLI NALS
