PHCA_GALSU
ID PHCA_GALSU Reviewed; 162 AA.
AC P00306;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=C-phycocyanin alpha chain;
GN Name=cpcA;
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.
RA Troxler R.F., Brown A.S.;
RT "Amino acid sequence of the phycocyanin alpha subunit from the alga,
RT Cyanidium caldarium.";
RL Fed. Proc. 38:325-325(1979).
RN [2]
RP PROTEIN SEQUENCE.
RX PubMed=7298651; DOI=10.1016/s0021-9258(18)43249-8;
RA Offner G.D., Brown-Mason A.S., Ehrhardt M.M., Troxler R.F.;
RT "Primary structure of phycocyanin from the unicellular rhodophyte Cyanidium
RT caldarium. I. Complete amino acid sequence of the alpha subunit.";
RL J. Biol. Chem. 256:12167-12175(1981).
RN [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 70-94, SUBUNIT, AND CHROMOPHORE ATTACHMENT AT CYS-84.
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 [6] {ECO:0007744|PDB:1PHN}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH CPCB AND
RP PHYCOCYANOBILIN, AND SUBUNIT.
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 [7] {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 [8] {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 (Ref.1,
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|Ref.1}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane;
CC Peripheral membrane protein; Stromal side. Note=Part of the
CC phycobilisome rod.
CC -!- PTM: Contains one covalently linked phycocyanobilin chromophore.
CC {ECO:0000269|PubMed:10354419, 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; AAB34028.1; -; mRNA.
DR EMBL; L13467; AAB01593.1; -; Genomic_DNA.
DR PDB; 1PHN; X-ray; 1.65 A; A=1-162.
DR PDB; 3BRP; X-ray; 1.85 A; A=1-162.
DR PDB; 3KVS; X-ray; 1.50 A; A=1-162.
DR PDBsum; 1PHN; -.
DR PDBsum; 3BRP; -.
DR PDBsum; 3KVS; -.
DR AlphaFoldDB; P00306; -.
DR SMR; P00306; -.
DR MINT; P00306; -.
DR STRING; 130081.XP_005704978.1; -.
DR PRIDE; P00306; -.
DR EvolutionaryTrace; P00306; -.
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; IPR006246; Phycocyanin_a.
DR Pfam; PF00502; Phycobilisome; 1.
DR PIRSF; PIRSF000081; Phycocyanin; 1.
DR SUPFAM; SSF46458; SSF46458; 1.
DR TIGRFAMs; TIGR01338; phycocy_alpha; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antenna complex; Bile pigment; Chloroplast; Chromophore;
KW Direct protein sequencing; Electron transport; Membrane; Photosynthesis;
KW Phycobilisome; Plastid; Thylakoid; Transport.
FT CHAIN 1..162
FT /note="C-phycocyanin alpha chain"
FT /id="PRO_0000199121"
FT BINDING 72..75
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT BINDING 83..87
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT BINDING 84
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000269|PubMed:10354419,
FT ECO:0000269|PubMed:468790, ECO:0007744|PDB:1PHN"
FT BINDING 128
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /evidence="ECO:0000269|PubMed:10354419"
FT CONFLICT 49
FT /note="E -> Q (in Ref. 4; AAB01593)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="S -> Q (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="V -> I (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="V -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:3KVS"
FT HELIX 21..46
FT /evidence="ECO:0007829|PDB:3KVS"
FT HELIX 48..62
FT /evidence="ECO:0007829|PDB:3KVS"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:3KVS"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:3KVS"
FT HELIX 78..101
FT /evidence="ECO:0007829|PDB:3KVS"
FT HELIX 105..110
FT /evidence="ECO:0007829|PDB:3KVS"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:3KVS"
FT HELIX 115..121
FT /evidence="ECO:0007829|PDB:3KVS"
FT HELIX 126..139
FT /evidence="ECO:0007829|PDB:3KVS"
FT HELIX 144..160
FT /evidence="ECO:0007829|PDB:3KVS"
SQ SEQUENCE 162 AA; 17506 MW; C941FDE84CDCBD95 CRC64;
MKTPITEAIA AADNQGRFLS NTELQAVNGR YQRAAASLEA ARSLTSNAER LINGAAQAVY
SKFPYTSQMP GPQYASSAVG KAKCARDIGY YLRMVTYCLV VGGTGPMDEY LIAGLEEINR
TFDLSPSWYV EALNYIKANH GLSGQAANEA NTYIDYAINA LS
