PHEB_CHRS2
ID PHEB_CHRS2 Reviewed; 177 AA.
AC U5T8F2;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Phycocyanin PC645 beta subunit {ECO:0000305};
OS Chroomonas sp. (strain CCMP270).
OG Plastid; Chloroplast {ECO:0000312|EMBL:AGY96986.1}.
OC Eukaryota; Cryptophyceae; Pyrenomonadales; Chroomonadaceae; Chroomonas;
OC unclassified Chroomonas.
OX NCBI_TaxID=354589;
RN [1] {ECO:0000312|EMBL:AGY96986.1, ECO:0007744|PDB:4LMS}
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN
RP COMPLEX WITH 15,16-DIHYDROBILIVERDIN; MESOBILIVERDIN AND PHYCOCYANOBILIN,
RP AND SUBUNIT.
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. {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 two phycocyanobilin chromophores, one mesobiliverdin
CC chromophore and one 15,16-dihydrobiliverdin chromophore 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 phycobiliprotein family. {ECO:0000305}.
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DR EMBL; KF314689; AGY96986.1; -; mRNA.
DR PDB; 4LMS; X-ray; 1.35 A; B/D=1-177.
DR PDBsum; 4LMS; -.
DR SMR; U5T8F2; -.
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="Phycocyanin PC645 beta subunit"
FT /id="PRO_0000455437"
FT BINDING 18
FT /ligand="mesobiliverdin"
FT /ligand_id="ChEBI:CHEBI:189061"
FT /ligand_note="ligand shared with alpha subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMS"
FT BINDING 28
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="1"
FT /ligand_note="ligand shared with alpha subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMS"
FT BINDING 35
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="1"
FT /ligand_note="ligand shared with alpha subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMS"
FT BINDING 39
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="1"
FT /ligand_note="ligand shared with alpha subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMS"
FT BINDING 50
FT /ligand="15,16-dihydrobiliverdin"
FT /ligand_id="ChEBI:CHEBI:57899"
FT /ligand_note="ligand shared with alpha subunit"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMS"
FT BINDING 54
FT /ligand="15,16-dihydrobiliverdin"
FT /ligand_id="ChEBI:CHEBI:57899"
FT /ligand_note="ligand shared with alpha subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMS"
FT BINDING 61
FT /ligand="15,16-dihydrobiliverdin"
FT /ligand_id="ChEBI:CHEBI:57899"
FT /ligand_note="ligand shared with alpha subunit"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMS"
FT BINDING 72
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="2"
FT /ligand_note="ligand shared with alpha subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMS"
FT BINDING 77
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="2"
FT /ligand_note="ligand shared with alpha subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMS"
FT BINDING 82
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
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:4LMS"
FT BINDING 84
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="2"
FT /ligand_note="ligand shared with alpha subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMS"
FT BINDING 85
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="2"
FT /ligand_note="ligand shared with alpha subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMS"
FT BINDING 148
FT /ligand="15,16-dihydrobiliverdin"
FT /ligand_id="ChEBI:CHEBI:57899"
FT /ligand_note="ligand shared with alpha subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMS"
FT BINDING 154
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="1"
FT /ligand_note="ligand shared with alpha subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMS"
FT BINDING 156
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="1"
FT /ligand_note="ligand shared with alpha subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMS"
FT BINDING 158
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="1"
FT /ligand_note="ligand shared with alpha subunit"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMS"
SQ SEQUENCE 177 AA; 18337 MW; 5E9292FD52B60B3B CRC64;
MLDAFSRVVT SADSKAAYVG GADLQALKKF VSEGNKRLDA VNAIVSNASC IVSDAVSGMI
CENPALISPS GNCYTNRRMA ACLRDAEIIL RYVSYSLLSG DSSVLEDRCL GGLKETYASL
GVPAAGNARA VGIMKATCVG FINNTSNQKK LSTPAGDCSA LASECAGYFD KVTSALA
