PHEB_HEMAN
ID PHEB_HEMAN Reviewed; 177 AA.
AC U5T8W0;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 2.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Phycoerythrin beta subunit {ECO:0000305};
DE AltName: Full=Phycoerythrin PE555 beta subunit {ECO:0000303|PubMed:24979784};
OS Hemiselmis andersenii (Cryptophyte alga).
OG Plastid; Chloroplast {ECO:0000312|EMBL:AGY96987.1}.
OC Eukaryota; Cryptophyceae; Cryptomonadales; Hemiselmidaceae; Hemiselmis.
OX NCBI_TaxID=464988 {ECO:0000312|EMBL:AGY96987.1};
RN [1] {ECO:0000312|EMBL:AGY96987.1, ECO:0007744|PDB:4LMX}
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN
RP COMPLEX WITH 15,16-DIHYDROBILIVERDIN AND PHYCOERYTHROBILIN, AND SUBUNIT.
RC STRAIN=CCMP644 {ECO:0000312|EMBL:AGY96987.1};
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 bile pigment-protein from the
CC 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 and one 15,16-
CC dihydrobiliverdin chromophore with binding of the phycoerythrobilin
CC chromophores 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 phycobiliprotein family. {ECO:0000305}.
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DR EMBL; KF314690; AGY96987.1; -; mRNA.
DR PDB; 4LMX; X-ray; 1.80 A; B/D/F/H/J/L=1-177.
DR PDBsum; 4LMX; -.
DR SMR; U5T8W0; -.
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; Electron transport;
KW Membrane; Photosynthesis; Plastid; Thylakoid; Transport.
FT CHAIN 1..177
FT /note="Phycoerythrin beta subunit"
FT /id="PRO_0000455438"
FT BINDING 18
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="1"
FT /ligand_note="ligand shared with alpha subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMX"
FT BINDING 28
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="2"
FT /ligand_note="ligand shared with alpha subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMX"
FT BINDING 35
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="2"
FT /ligand_note="ligand shared with alpha subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMX"
FT BINDING 39
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="2"
FT /ligand_note="ligand shared with alpha subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMX"
FT BINDING 50
FT /ligand="15,16-dihydrobiliverdin"
FT /ligand_id="ChEBI:CHEBI:57899"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMX"
FT BINDING 54
FT /ligand="15,16-dihydrobiliverdin"
FT /ligand_id="ChEBI:CHEBI:57899"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMX"
FT BINDING 61
FT /ligand="15,16-dihydrobiliverdin"
FT /ligand_id="ChEBI:CHEBI:57899"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMX"
FT BINDING 82
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="3"
FT /ligand_note="ligand shared with alpha subunit"
FT /note="covalent"
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="3"
FT /ligand_note="ligand shared with alpha subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMX"
FT BINDING 85
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="3"
FT /ligand_note="ligand shared with alpha subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMX"
FT BINDING 129
FT /ligand="15,16-dihydrobiliverdin"
FT /ligand_id="ChEBI:CHEBI:57899"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMX"
FT BINDING 144
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="2"
FT /ligand_note="ligand shared with alpha subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMX"
FT BINDING 148
FT /ligand="15,16-dihydrobiliverdin"
FT /ligand_id="ChEBI:CHEBI:57899"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMX"
FT BINDING 149
FT /ligand="15,16-dihydrobiliverdin"
FT /ligand_id="ChEBI:CHEBI:57899"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMX"
FT BINDING 154
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="2"
FT /ligand_note="ligand shared with alpha subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMX"
FT BINDING 156
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="2"
FT /ligand_note="ligand shared with alpha subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMX"
FT BINDING 158
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /ligand_label="2"
FT /ligand_note="ligand shared with alpha subunit"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMX"
FT CONFLICT 172
FT /note="V -> E (in Ref. 1; AGY96987)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 177 AA; 18390 MW; F8AF688D4ADDF648 CRC64;
MLDAFSKVIT SADGKAAYVG GADLQALKKF VSEGNKRMDS VNAIVSNASC IVSDSVSGMV
CENPSLIAPN GGVYTNRKMA ACLRDAEIIL RYVSYSLLSG DSSVLEDRCL NGLKETYASL
GVPAAGNART ISIMKATVIG FITNNSQQKK LSTPAGDCSA LASEVGGYFD KVSSALA
