PHEA1_HEMAN
ID PHEA1_HEMAN Reviewed; 114 AA.
AC U5TBU5;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Phycoerythrin alpha-1 subunit {ECO:0000305};
DE AltName: Full=Phycoerythrin PE555 alpha-1 subunit {ECO:0000305};
DE Short=PE555A-1 {ECO:0000303|PubMed:24979784};
OS Hemiselmis andersenii (Cryptophyte alga).
OG Plastid; Chloroplast {ECO:0000312|EMBL:AGY96993.1}.
OC Eukaryota; Cryptophyceae; Cryptomonadales; Hemiselmidaceae; Hemiselmis.
OX NCBI_TaxID=464988 {ECO:0000312|EMBL:AGY96993.1};
RN [1] {ECO:0000312|EMBL:AGY96993.1, ECO:0007744|PDB:4LMX}
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF
RP 48-114 IN COMPLEX WITH PHYCOERYTHROBILIN, AND SUBUNIT.
RC STRAIN=CCMP644 {ECO:0000312|EMBL:AGY96993.1};
RX PubMed=24979784; DOI=10.1073/pnas.1402538111;
RA Harrop S.J., Wilk K.E., Dinshaw R., Collini E., Mirkovic T., Teng C.Y.,
RA Oblinsky D.G., Green B.R., Hoef-Emden K., Hiller R.G., Scholes G.D.,
RA Curmi P.M.;
RT "Single-residue insertion switches the quaternary structure and exciton
RT states of cryptophyte light-harvesting proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E2666-E2675(2014).
CC -!- FUNCTION: Light-harvesting photosynthetic tetrapyrrole chromophore-
CC protein from the phycobiliprotein complex. {ECO:0000305}.
CC -!- SUBUNIT: Heterotetramer of 2 different alpha chains and 2 identical
CC beta chains which form 2 alpha-beta heterodimers within the
CC heterotetramer. The two alpha-beta heterodimers are rotated to an open
CC configuration in contrast to the closed configuration found in other
CC cryptophyte species due to the insertion of a single amino acid, Asp-
CC 65, in a conserved region of the alpha chain. In the open form, the
CC central chromophores are not in physical contact but are separated by a
CC water-filled channel. {ECO:0000269|PubMed:24979784}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Lumenal side
CC {ECO:0000305}.
CC -!- PTM: Contains three phycoerythrobilin chromophores with binding
CC mediated by both the alpha and beta subunits.
CC {ECO:0000269|PubMed:24979784}.
CC -!- MISCELLANEOUS: The light-harvesting system in Cryptophytes contains
CC phycobiliprotein complexes. Unusually they are composed of either
CC phycoerythrin (CPE) or phycocyanin (CPC) but never allophycocyanin
CC (APC), with only one type of biliprotein being present in any one
CC species. Unlike cyanobacteria or red algae these proteins are not
CC arranged into higher-order phycobilisome complexes, and they are found
CC in the thylakoid lumen. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the phycoerythrin family. {ECO:0000305}.
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DR EMBL; KF314696; AGY96993.1; -; mRNA.
DR PDB; 4LMX; X-ray; 1.80 A; C=48-114.
DR PDBsum; 4LMX; -.
DR SMR; U5TBU5; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030089; C:phycobilisome; IEA:InterPro.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.510.10; -; 1.
DR InterPro; IPR011070; Globular_prot_asu/bsu.
DR InterPro; IPR037011; Phycoerythr-like_a_sf.
DR InterPro; IPR004228; Phycoerythr_a.
DR Pfam; PF02972; Phycoerythr_ab; 1.
DR SUPFAM; SSF56568; SSF56568; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bile pigment; Chloroplast; Chromophore; Electron transport;
KW Membrane; Photosynthesis; Plastid; Thylakoid; Transport.
FT CHAIN 1..114
FT /note="Phycoerythrin alpha-1 subunit"
FT /id="PRO_5004664522"
FT BINDING 52
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="1"
FT /ligand_note="ligand shared with beta subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMX"
FT BINDING 53
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="1"
FT /ligand_note="ligand shared with beta subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMX"
FT BINDING 63
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="2"
FT /ligand_note="ligand shared with beta subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMX"
FT BINDING 64
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="3"
FT /ligand_note="ligand shared with beta subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMX"
FT BINDING 67
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="2"
FT /ligand_note="ligand shared with beta subunit"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMX"
FT BINDING 72
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="2"
FT /ligand_note="ligand shared with beta subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMX"
FT BINDING 74
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="2"
FT /ligand_note="ligand shared with beta subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMX"
FT BINDING 75
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="2"
FT /ligand_note="ligand shared with beta subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMX"
FT BINDING 84
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="2"
FT /ligand_note="ligand shared with beta subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMX"
SQ SEQUENCE 114 AA; 11634 MW; A87F9E87B43F609C CRC64;
MYTKIALLGL VGSAAAFNAP MMTVRRDAIA TGAAAAVVAP MLRPAGAAMK KDSKAPCVEV
FDERDGCKAA GTQKASGDDG FCVKVSMKAI GFNAAEAASV TKNYGIKRFG AKSV
