PHE2_RHDS2
ID PHE2_RHDS2 Reviewed; 104 AA.
AC P30943; Q8VX02;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Phycoerythrin alpha-2 chain, chloroplastic;
DE Flags: Precursor;
GN Name=cpeA2;
OS Rhodomonas sp. (strain CS 24) (Chroomonas sp. (strain CS24)).
OC Eukaryota; Cryptophyceae; Pyrenomonadales; Pyrenomonadaceae; Rhodomonas;
OC unclassified Rhodomonas.
OX NCBI_TaxID=79257;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hiller R.G., Howe C.E.;
RT "Nuclear-encoded genes of phycoerythrin alpha subunits.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 38-82.
RX PubMed=2226853; DOI=10.1016/0014-5793(90)81082-y;
RA Jenkins J., Hiller R.G., Speirs J., Godovac-Zimmermann J.;
RT "A genomic clone encoding a cryptophyte phycoerythrin alpha-subunit.
RT Evidence for three alpha-subunits and an N-terminal membrane transit
RT sequence.";
RL FEBS Lett. 273:191-194(1990).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 38-104 IN COMPLEX WITH CPEA2;
RP CPEA3 AND 15,16-DIHYDROBILIVERDIN, SUBUNIT, AND HYDROXYLATION AT LYS-41.
RX PubMed=10430868; DOI=10.1073/pnas.96.16.8901;
RA Wilk K.E., Harrop S.J., Jankova L., Edler D., Keenan G., Sharples F.,
RA Hiller R.G., Curmi P.M.;
RT "Evolution of a light-harvesting protein by addition of new subunits and
RT rearrangement of conserved elements: crystal structure of a cryptophyte
RT phycoerythrin at 1.63-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:8901-8906(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (0.97 ANGSTROMS) OF 38-104 IN COMPLEX WITH CPEA2;
RP CPEA3 AND 15,16-DIHYDROBILIVERDIN, AND SUBUNIT.
RX PubMed=15504407; DOI=10.1016/j.jmb.2004.09.044;
RA Doust A.B., Marai C.N., Harrop S.J., Wilk K.E., Curmi P.M., Scholes G.D.;
RT "Developing a structure-function model for the cryptophyte phycoerythrin
RT 545 using ultrahigh resolution crystallography and ultrafast laser
RT spectroscopy.";
RL J. Mol. Biol. 344:135-153(2004).
CC -!- FUNCTION: Light-harvesting photosynthetic tetrapyrrole chromophore-
CC protein from the phycobiliprotein complex.
CC -!- SUBUNIT: Heterotetramer of 2 different alpha chains and 2 identical
CC beta chains. The subunit composition could comprise of any combination
CC of 2 out of 4 different alpha units with an invariant beta unit.
CC {ECO:0000269|PubMed:10430868, ECO:0000269|PubMed:15504407}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane;
CC Peripheral membrane protein; Lumenal side.
CC -!- PTM: Contains one covalently linked 15,16-dihydrobiliverdin
CC chromophore.
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.
CC -!- SIMILARITY: Belongs to the phycoerythrin family. {ECO:0000305}.
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DR EMBL; AJ006994; CAD20039.1; -; Genomic_DNA.
DR PIR; T10881; T10881.
DR PDB; 1QGW; X-ray; 1.63 A; B=38-104.
DR PDB; 1XF6; X-ray; 1.10 A; B=38-104.
DR PDB; 1XG0; X-ray; 0.97 A; B=38-104.
DR PDBsum; 1QGW; -.
DR PDBsum; 1XF6; -.
DR PDBsum; 1XG0; -.
DR AlphaFoldDB; P30943; -.
DR SMR; P30943; -.
DR EvolutionaryTrace; P30943; -.
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;
KW Direct protein sequencing; Electron transport; Hydroxylation; Membrane;
KW Photosynthesis; Plastid; Thylakoid; Transit peptide; Transport.
FT TRANSIT 1..37
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:2226853"
FT CHAIN 38..104
FT /note="Phycoerythrin alpha-2 chain, chloroplastic"
FT /id="PRO_0000002827"
FT REGION 61..63
FT /note="15,16-dihydrobiliverdin chromophore"
FT BINDING 56
FT /ligand="15,16-dihydrobiliverdin"
FT /ligand_id="ChEBI:CHEBI:57899"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000269|PubMed:10430868,
FT ECO:0000269|PubMed:15504407"
FT BINDING 58
FT /ligand="15,16-dihydrobiliverdin"
FT /ligand_id="ChEBI:CHEBI:57899"
FT /evidence="ECO:0000269|PubMed:10430868,
FT ECO:0000269|PubMed:15504407"
FT BINDING 78
FT /ligand="15,16-dihydrobiliverdin"
FT /ligand_id="ChEBI:CHEBI:57899"
FT /evidence="ECO:0000269|PubMed:10430868,
FT ECO:0000269|PubMed:15504407"
FT MOD_RES 41
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:10430868"
FT CONFLICT 63..74
FT /note="YTGAKAGGKDDE -> TSKSGKSGQDDT (in Ref. 2; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT STRAND 44..52
FT /evidence="ECO:0007829|PDB:1XG0"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:1XG0"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:1XG0"
FT HELIX 88..101
FT /evidence="ECO:0007829|PDB:1XG0"
SQ SEQUENCE 104 AA; 10696 MW; 1474D433E8CB4396 CRC64;
MSAKIIAFSA VVATASAFAP TAGFVPRLRS GATSVNMAMD KSAKAPVITI FDHRGCSRAP
KEYTGAKAGG KDDEMMVKAQ SVKIEVSTGT AEGVLATSLA KMTK