PHCB_GALSU
ID PHCB_GALSU Reviewed; 172 AA.
AC P00311;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 4.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=C-phycocyanin beta chain;
GN Name=cpcB;
OS Galdieria sulphuraria (Red alga).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Galdieria.
OX NCBI_TaxID=130081;
RN [1]
RP PROTEIN SEQUENCE, AND SUBUNIT.
RX PubMed=7028751; DOI=10.1016/s0021-9258(18)43250-4;
RA Troxler R.F., Ehrhardt M.M., Brown-Mason A.S., Offner G.D.;
RT "Primary structure of phycocyanin from the unicellular rhodophyte Cyanidium
RT caldarium. II. Complete amino acid sequence of the beta subunit.";
RL J. Biol. Chem. 256:12176-12184(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=III-D-2;
RX PubMed=7716249; DOI=10.1104/pp.107.3.985;
RA Troxler R.F., Yan Y., Jiang J.W., Liu B.;
RT "Nucleotide sequence and expression of the genes for the alpha and beta
RT subunits of phycocyanin in Cyanidium caldarium.";
RL Plant Physiol. 107:985-994(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=III-D-2;
RA Troxler R.F., Yan Y., Zhang F., Jiang J.-W.;
RT "Heme regulated photogenes in the unicellular rhodophyte, Cyanidium
RT caldarium. Cloning and nucleotide sequence of genes for phycocyanin.";
RL Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 80-86 AND 136-166, SUBUNIT, AND CHROMOPHORE ATTACHMENT
RP AT CYS-82 AND CYS-153.
RC STRAIN=Allen;
RX PubMed=468790; DOI=10.1016/s0021-9258(18)36018-6;
RA Brown A.S., Offner G.D., Ehrhardt M.M., Troxler R.F.;
RT "Phycobilin-apoprotein linkages in the alpha and beta subunits of
RT phycocyanin from the unicellular rhodophyte, Cyanidium caldarium. Amino
RT acid sequences of 35S-labeled chromopeptides.";
RL J. Biol. Chem. 254:7803-7811(1979).
RN [5] {ECO:0007744|PDB:1PHN}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH CPCA AND
RP PHYCOCYANOBILIN, SUBUNIT, AND METHYLATION AT ASN-72.
RX PubMed=10354419; DOI=10.1016/s0006-3495(99)77446-1;
RA Stec B., Troxler R.F., Teeter M.M.;
RT "Crystal structure of C-phycocyanin from Cyanidium caldarium provides a new
RT perspective on phycobilisome assembly.";
RL Biophys. J. 76:2912-2921(1999).
RN [6] {ECO:0007744|PDB:3BRP}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RA Fromme R., Thangaraj B., Vanselow C., Fromme P.;
RT "Crystal Structure of C-Phycocyanin from Galdieria sulphuraria at 1.85 A.";
RL Submitted (DEC-2007) to the PDB data bank.
RN [7] {ECO:0007744|PDB:3KVS}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS).
RA Fromme R., Thangaraj B., Vanselow C., Fromme P.;
RT "High resolution structure of C-Phycocyanin from Galdieria sulphuraria
RT reveals new insights of the Phycobilisome.";
RL Submitted (NOV-2009) to the PDB data bank.
CC -!- FUNCTION: Light-harvesting photosynthetic tetrapyrrole chromophore-
CC protein from the phycobiliprotein complex (phycobilisome, PBS).
CC Phycocyanin is the major phycobiliprotein in the PBS rod.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit (PubMed:7028751,
CC PubMed:468790, PubMed:10354419). Dimers further assemble into trimers
CC and the trimers into hexamers. The basic functional unit of
CC phycobiliproteins is a ring-shaped hexamer formed from two back-to-back
CC trimers contacting via the alpha chain subunits. The trimers are
CC composed of alpha/beta subunit heterodimers arranged around a three-
CC fold axis of symmetry. The phycoerythrins also contain a gamma subunit
CC which is located in the center of the hexamer (PubMed:10354419).
CC {ECO:0000269|PubMed:10354419, ECO:0000269|PubMed:468790,
CC ECO:0000269|PubMed:7028751}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane;
CC Peripheral membrane protein; Stromal side. Note=Part of the
CC phycobilisome rod.
CC -!- PTM: Contains two covalently linked phycocyanobilin chromophores.
CC {ECO:0000269|PubMed:468790}.
CC -!- MISCELLANEOUS: The light-harvesting antenna system in red algae and
CC cyanobacteria is formed of phycobilisomes. These are composed of the
CC phycobiliproteins phycoerythrin (CPE), phycocyanin (CPC) and
CC allophycocyanin (APC). Cyanobacteria also contain phycoerythrocyanin
CC (PCC). The phycobiliproteins all share the same subunit composition and
CC organization with variations in the covalently bound open-chain
CC tetrapyrrole chromophores. The phycobiliprotein complexes are arranged
CC sequentially in antenna complexes linked by linker proteins with CPE at
CC the periphery, CPC in the middle and APC at the core feeding to the
CC photosynthetic reaction center.
CC -!- MISCELLANEOUS: Although originally identified as Cyanidium caldarium,
CC these sequences derive from Galdieria sulphuraria. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the phycobiliprotein family. {ECO:0000305}.
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DR EMBL; S77125; AAB34027.2; -; mRNA.
DR EMBL; L13467; AAB01592.1; -; Genomic_DNA.
DR PIR; A00320; CFKKB.
DR PDB; 1PHN; X-ray; 1.65 A; B=1-172.
DR PDB; 3BRP; X-ray; 1.85 A; B=1-172.
DR PDB; 3KVS; X-ray; 1.50 A; B=1-172.
DR PDBsum; 1PHN; -.
DR PDBsum; 3BRP; -.
DR PDBsum; 3KVS; -.
DR AlphaFoldDB; P00311; -.
DR SMR; P00311; -.
DR MINT; P00311; -.
DR STRING; 130081.XP_005704979.1; -.
DR iPTMnet; P00311; -.
DR eggNOG; ENOG502SQCB; Eukaryota.
DR EvolutionaryTrace; P00311; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030089; C:phycobilisome; IEA:UniProtKB-KW.
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 InterPro; IPR006247; Phycocyanin_b.
DR Pfam; PF00502; Phycobilisome; 1.
DR PIRSF; PIRSF000081; Phycocyanin; 1.
DR SUPFAM; SSF46458; SSF46458; 1.
DR TIGRFAMs; TIGR01339; phycocy_beta; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antenna complex; Bile pigment; Chloroplast; Chromophore;
KW Direct protein sequencing; Electron transport; Membrane; Methylation;
KW Photosynthesis; Phycobilisome; Plastid; Thylakoid; Transport.
FT CHAIN 1..172
FT /note="C-phycocyanin beta chain"
FT /id="PRO_0000199149"
FT BINDING 35
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10354419"
FT BINDING 39
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10354419"
FT BINDING 72
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10354419"
FT BINDING 77
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10354419"
FT BINDING 82..88
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="2"
FT BINDING 82
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="2"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000269|PubMed:10354419,
FT ECO:0000269|PubMed:468790"
FT BINDING 149..151
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="1"
FT BINDING 153
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="1"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000269|PubMed:10354419,
FT ECO:0000269|PubMed:468790"
FT MOD_RES 72
FT /note="N4-methylasparagine"
FT /evidence="ECO:0000269|PubMed:10354419"
FT CONFLICT 72
FT /note="N -> I (in Ref. 2; AAB01592)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="N -> T (in Ref. 2; AAB34027 and 1; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="I -> V (in Ref. 2; AAB01592)"
FT /evidence="ECO:0000305"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:3KVS"
FT HELIX 21..32
FT /evidence="ECO:0007829|PDB:3KVS"
FT HELIX 34..46
FT /evidence="ECO:0007829|PDB:3KVS"
FT HELIX 48..62
FT /evidence="ECO:0007829|PDB:3KVS"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:3KVS"
FT HELIX 76..99
FT /evidence="ECO:0007829|PDB:3KVS"
FT HELIX 103..108
FT /evidence="ECO:0007829|PDB:3KVS"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:3KVS"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:3KVS"
FT HELIX 124..142
FT /evidence="ECO:0007829|PDB:3KVS"
FT HELIX 154..170
FT /evidence="ECO:0007829|PDB:3KVS"
SQ SEQUENCE 172 AA; 18253 MW; F271B4D8CD5963CD CRC64;
MLDAFAKVVA QADARGEFLS NTQLDALSKM VSEGNKRLDV VNRITSNASA IVTNAARALF
SEQPQLIQPG GNAYTNRRMA ACLRDMEIIL RYVSYAIIAG DSSILDDRCL NGLRETYQAL
GVPGASVAVG IEKMKDSAIA IANDPSGITT GDCSALMAEV GTYFDRAATA VQ
