PHEB_CHRSP
ID PHEB_CHRSP Reviewed; 177 AA.
AC P23817;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Phycocyanin-645 beta chain;
DE Short=PC-645;
OS Chroomonas sp.
OC Eukaryota; Cryptophyceae; Pyrenomonadales; Chroomonadaceae; Chroomonas;
OC unclassified Chroomonas.
OX NCBI_TaxID=3029;
RN [1]
RP PROTEIN SEQUENCE, AND CHROMOPHORE BINDING AT CYS-50; CYS-61; CYS-82 AND
RP CYS-158.
RX PubMed=2222853; DOI=10.1515/bchm3.1990.371.2.537;
RA Sidler W., Nutt H., Kumpf B., Frank G., Suter F., Brenzel A., Wehrmeyer W.,
RA Zuber H.;
RT "The complete amino-acid sequence and the phylogenetic origin of
RT phycocyanin-645 from the cryptophytan alga Chroomonas sp.";
RL Biol. Chem. Hoppe-Seyler 371:537-547(1990).
RN [2]
RP PROTEIN SEQUENCE OF 1-43.
RX PubMed=4005040; DOI=10.1515/bchm3.1985.366.1.233;
RA Sidler W., Kumpf B., Suter F., Morisset W., Wehrmeyer W., Zuber H.;
RT "Structural studies on cryptomonad biliprotein subunits. Two different
RT alpha-subunits in Chroomonas phycocyanin-645 and Cryptomonas phycoerythrin-
RT 545.";
RL Biol. Chem. Hoppe-Seyler 366:233-244(1985).
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:0000250|UniProtKB:U5T8F2}.
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:0000250|UniProtKB:U5T8F2}.
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 PIR; S10604; E22102.
DR AlphaFoldDB; P23817; -.
DR SMR; P23817; -.
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 Bile pigment; Chloroplast; Chromophore; Direct protein sequencing;
KW Electron transport; Membrane; Photosynthesis; Plastid; Thylakoid;
KW Transport.
FT CHAIN 1..177
FT /note="Phycocyanin-645 beta chain"
FT /id="PRO_0000199208"
FT BINDING 18
FT /ligand="mesobiliverdin"
FT /ligand_id="ChEBI:CHEBI:189061"
FT /ligand_note="ligand shared with alpha subunit"
FT /evidence="ECO:0000250|UniProtKB:U5T8F2"
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:0000250|UniProtKB:U5T8F2"
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:0000250|UniProtKB:U5T8F2"
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:0000250|UniProtKB:U5T8F2"
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:0000250|UniProtKB:U5T8F2"
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:0000250|UniProtKB:U5T8F2"
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:0000250|UniProtKB:U5T8F2"
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:0000250|UniProtKB:U5T8F2"
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:0000250|UniProtKB:U5T8F2"
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:0000250|UniProtKB:U5T8F2"
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:0000250|UniProtKB:U5T8F2"
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:0000250|UniProtKB:U5T8F2"
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:0000250|UniProtKB:U5T8F2"
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:0000250|UniProtKB:U5T8F2"
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:0000250|UniProtKB:U5T8F2"
SQ SEQUENCE 177 AA; 18388 MW; 56497A55F992FA7F CRC64;
MLDAFSRVVT GADSKAAYVG GADLQALKKF VSEGNKRLDA VNAIVSNASC IVSDAVSGMI
CENPSLISPS GECYTNRRMA ACLRDAEIIL RYVSYSLLSG DSSVLEDRCL SGLKETYASL
GVPAAGNARA VGIMKATVVA FINNTSNQKK LLTPSGDCSA LASEAAGYFD KVTSALA
