PHEA1_HEMVI
ID PHEA1_HEMVI Reviewed; 109 AA.
AC C0HM11; A0A075B5G1; A0A075BTU2;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 1.
DT 03-AUG-2022, entry version 2.
DE RecName: Full=Phycoerythrin alpha-1 subunit {ECO:0000305};
GN Name=cpeA1 {ECO:0000312|EMBL:AGR45601.1};
OS Hemiselmis virescens.
OG Plastid; Chloroplast {ECO:0000305}.
OC Eukaryota; Cryptophyceae; Cryptomonadales; Hemiselmidaceae; Hemiselmis.
OX NCBI_TaxID=77927;
RN [1] {ECO:0000312|EMBL:AGR45601.1}
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF
RP 48-109 IN COMPLEX WITH PHYCOCYANOBILIN, AND SUBUNIT.
RC STRAIN=M1635 {ECO:0000312|EMBL:AGR45601.1};
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 identical 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 phycocyanobilin chromophores with binding mediated
CC by both the alpha and beta subunits. {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; KC905456; AGR45601.1; -; mRNA.
DR PDB; 4LM6; X-ray; 1.70 A; A/C=48-109.
DR PDBsum; 4LM6; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
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 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..109
FT /note="Phycoerythrin alpha-1 subunit"
FT /id="PRO_5007375773"
FT BINDING 6
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="1"
FT /ligand_note="ligand shared with beta subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LM6"
FT BINDING 16
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="3"
FT /ligand_note="ligand shared with beta subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LM6"
FT BINDING 17
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="2"
FT /ligand_note="ligand shared with beta subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LM6"
FT BINDING 20
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="3"
FT /ligand_note="ligand shared with beta subunit"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LM6"
FT BINDING 27
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="3"
FT /ligand_note="ligand shared with beta subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LM6"
FT BINDING 28
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="3"
FT /ligand_note="ligand shared with beta subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LM6"
FT BINDING 39
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="3"
FT /ligand_note="ligand shared with beta subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LM6"
SQ SEQUENCE 109 AA; 11173 MW; B0328C6DFD868087 CRC64;
MYTKAVLLAF VGSAAAFNAP MMTVRRDAIA TGAAAAVVAP LLRPAGAKMA TDSKAPLIEL
FDERDGCKGP AANKASDVGE PGLCVKVSMQ KVAMNAAAAK SVATNYMRK
