PHEB_RHDS2
ID PHEB_RHDS2 Reviewed; 177 AA.
AC P27198;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=B-phycoerythrin beta chain;
GN Name=cpeB;
OS Rhodomonas sp. (strain CS 24) (Chroomonas sp. (strain CS24)).
OG Plastid; Chloroplast.
OC Eukaryota; Cryptophyceae; Pyrenomonadales; Pyrenomonadaceae; Rhodomonas;
OC unclassified Rhodomonas.
OX NCBI_TaxID=79257;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=1554738; DOI=10.1016/0167-4838(92)90432-d;
RA Godovac-Zimmermann J., Sheil M., Wrench P.M., Hiller R.G.;
RT "Amino acid sequence of the beta-subunit of phycoerythrin from the
RT cryptophyte algae Chroomonas CS 24.";
RL Biochim. Biophys. Acta 1120:117-121(1992).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) IN COMPLEX WITH CPEA2; CPEA3 AND
RP PHYCOERYTHROBILIN, SUBUNIT, AND METHYLATION AT ASN-72.
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 [3]
RP X-RAY CRYSTALLOGRAPHY (0.97 ANGSTROMS) IN COMPLEX WITH CPEA2; CPEA3 AND
RP PHYCOERYTHROBILIN, SUBUNIT, AND METHYLATION AT ASN-72.
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 any combination of
CC 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 three covalently linked phycoerythrobilin chromophores.
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 phycobiliprotein family. {ECO:0000305}.
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DR PDB; 1QGW; X-ray; 1.63 A; C/D=1-177.
DR PDB; 1XF6; X-ray; 1.10 A; C/D=1-177.
DR PDB; 1XG0; X-ray; 0.97 A; C/D=1-177.
DR PDBsum; 1QGW; -.
DR PDBsum; 1XF6; -.
DR PDBsum; 1XG0; -.
DR AlphaFoldDB; P27198; -.
DR SMR; P27198; -.
DR iPTMnet; P27198; -.
DR EvolutionaryTrace; P27198; -.
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; 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; Bile pigment; Chloroplast; Chromophore;
KW Direct protein sequencing; Electron transport; Membrane; Methylation;
KW Photosynthesis; Plastid; Thylakoid; Transport.
FT CHAIN 1..177
FT /note="B-phycoerythrin beta chain"
FT /id="PRO_0000199200"
FT BINDING 28
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:10430868,
FT ECO:0000269|PubMed:15504407"
FT BINDING 35
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:10430868,
FT ECO:0000269|PubMed:15504407"
FT BINDING 39
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:10430868,
FT ECO:0000269|PubMed:15504407"
FT BINDING 50
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="1"
FT /note="covalent, via 2 links"
FT /evidence="ECO:0000269|PubMed:10430868,
FT ECO:0000269|PubMed:15504407"
FT BINDING 54
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10430868,
FT ECO:0000269|PubMed:15504407"
FT BINDING 61
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="1"
FT /note="covalent, via 2 links"
FT /evidence="ECO:0000269|PubMed:10430868,
FT ECO:0000269|PubMed:15504407"
FT BINDING 72
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10430868,
FT ECO:0000269|PubMed:15504407"
FT BINDING 77..78
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="2"
FT BINDING 82
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="2"
FT BINDING 82
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:10430868,
FT ECO:0000269|PubMed:15504407"
FT BINDING 129
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10430868,
FT ECO:0000269|PubMed:15504407"
FT BINDING 147..148
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="1"
FT BINDING 154..158
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="3"
FT BINDING 158
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="3"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000269|PubMed:10430868,
FT ECO:0000269|PubMed:15504407"
FT MOD_RES 72
FT /note="N4-methylasparagine"
FT /evidence="ECO:0000269|PubMed:10430868,
FT ECO:0000269|PubMed:15504407"
FT CONFLICT 50
FT /note="C -> V (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="V -> Y (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="C -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="S -> H (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="C -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 4..9
FT /evidence="ECO:0007829|PDB:1XG0"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:1XG0"
FT HELIX 22..30
FT /evidence="ECO:0007829|PDB:1XG0"
FT HELIX 34..45
FT /evidence="ECO:0007829|PDB:1XG0"
FT HELIX 48..62
FT /evidence="ECO:0007829|PDB:1XG0"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:1XG0"
FT HELIX 76..99
FT /evidence="ECO:0007829|PDB:1XG0"
FT HELIX 103..108
FT /evidence="ECO:0007829|PDB:1XG0"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:1XG0"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:1XG0"
FT HELIX 124..142
FT /evidence="ECO:0007829|PDB:1XG0"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:1XG0"
FT HELIX 159..176
FT /evidence="ECO:0007829|PDB:1XG0"
SQ SEQUENCE 177 AA; 18508 MW; 51008EFCF1D7C717 CRC64;
MLDAFSRVVT NADSKAAYVG GADLQALKKF ISEGNKRLDS VNSIVSNASC IVSDAVSGMI
CENPSLISPS GNCYTNRRMA ACLRDGEIIL RYVSYALLSG DASVLEDRCL NGLKETYSSL
GVPANSNARA VSIMKACAVA FVNNTASQKK LSTPQGDCSG LASEVGGYFD KVTAAIS
