PHCA_ARTPT
ID PHCA_ARTPT Reviewed; 162 AA.
AC P72509;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=C-phycocyanin alpha subunit;
GN Name=cpcA;
OS Arthrospira platensis (Spirulina platensis).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC Microcoleaceae; Arthrospira.
OX NCBI_TaxID=118562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C1;
RA Jeamton W., Chaisawadi S., Deshnium P., Castets A.M., Coursin T.,
RA Tandeau de Marsac N., Tanticharoen M., Cheevadhanarak S.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:1GH0}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH PHYCOCYANOBILIN
RP CHROMOPHORE, SUBUNIT, AND SEQUENCE REVISION TO 51.
RX PubMed=11375497; DOI=10.1107/s0907444901004528;
RA Wang X.Q., Li L.N., Chang W.R., Zhang J.P., Gui L.L., Guo B.J., Liang D.C.;
RT "Structure of C-phycocyanin from Spirulina platensis at 2.2 A resolution: a
RT novel monoclinic crystal form for phycobiliproteins in phycobilisomes.";
RL Acta Crystallogr. D 57:784-792(2001).
RN [3] {ECO:0007744|PDB:1HA7}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH PHYCOCYANOBILIN
RP CHROMOPHORE, AND SEQUENCE REVISION TO 51 AND 148.
RX PubMed=11352634; DOI=10.1006/bbrc.2001.4663;
RA Padyana A.K., Bhat V.B., Madhyasta K.M., Rajashankar K.R., Ramakumar S.;
RT "Crystal structure of a light-harvesting protein C-phycocyanin from
RT Spirulina platensis.";
RL Biochem. Biophys. Res. Commun. 282:893-898(2001).
RN [4] {ECO:0007744|PDB:2UUM}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH PHYCOCYANOBILIN
RP CHROMOPHORE, AND SUBUNIT.
RA Satyanarayana L., Patel A., Mishra S., Ghosh P.K., Suresh C.G.;
RT "Crystal Structure of C-Phycocyanin from Phormidium, Lyngbya Spp. (Marine)
RT and Spirulina Sp. (Fresh Water) Shows Two Different Ways of Energy Transfer
RT between Two Hexamers.";
RL Submitted (MAR-2007) to the PDB data bank.
CC -!- FUNCTION: Light-harvesting photosynthetic bile pigment-protein from the
CC phycobiliprotein complex (phycobilisome, PBS). Phycocyanin is the major
CC phycobiliprotein in the PBS rod.
CC -!- SUBUNIT: The alpha and beta subunits exhibit high affinity for one
CC another and form heterodimers. These heterodimers form heterohexamers
CC of 3 alpha and 3 beta subunits which, in turn, aggregate into a
CC heterododecamer consisting of 2 heterohexamers.
CC {ECO:0000269|PubMed:11352634, ECO:0000269|PubMed:11375497}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane
CC protein; Cytoplasmic side. Note=Part of the phycobilisome rod.
CC -!- PTM: Contains one covalently linked phycocyanobilin chromophore.
CC {ECO:0000269|PubMed:11352634, ECO:0000269|PubMed:11375497,
CC ECO:0007744|PDB:1GH0, ECO:0007744|PDB:1HA7, ECO:0007744|PDB:2UUM}.
CC -!- SIMILARITY: Belongs to the phycobiliprotein family. {ECO:0000305}.
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DR EMBL; Y09074; CAA70296.1; -; Genomic_DNA.
DR PDB; 1GH0; X-ray; 2.20 A; A/C/E/G/I/K/M/O/Q/S/U/W=1-162.
DR PDB; 1HA7; X-ray; 2.20 A; A/C/E/G/I/K/M/O/Q/S/U/W=1-162.
DR PDB; 2UUM; X-ray; 3.00 A; A/C/E/G/I/K/M/O/Q/S/U/W=1-162.
DR PDBsum; 1GH0; -.
DR PDBsum; 1HA7; -.
DR PDBsum; 2UUM; -.
DR AlphaFoldDB; P72509; -.
DR SMR; P72509; -.
DR EvolutionaryTrace; P72509; -.
DR GO; GO:0030089; C:phycobilisome; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
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; Chromophore;
KW Electron transport; Membrane; Photosynthesis; Phycobilisome; Thylakoid;
KW Transport.
FT CHAIN 1..162
FT /note="C-phycocyanin alpha subunit"
FT /id="PRO_0000199127"
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:11352634,
FT ECO:0000269|PubMed:11375497, ECO:0007744|PDB:1GH0,
FT ECO:0007744|PDB:1HA7, ECO:0007744|PDB:2UUM"
FT CONFLICT 51
FT /note="L -> R (in Ref. 1; CAA70296)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="T -> G (in Ref. 1; CAA70296)"
FT /evidence="ECO:0000305"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:1GH0"
FT HELIX 21..46
FT /evidence="ECO:0007829|PDB:1GH0"
FT HELIX 48..62
FT /evidence="ECO:0007829|PDB:1GH0"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:1GH0"
FT HELIX 78..101
FT /evidence="ECO:0007829|PDB:1GH0"
FT HELIX 105..110
FT /evidence="ECO:0007829|PDB:1GH0"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:1GH0"
FT HELIX 115..121
FT /evidence="ECO:0007829|PDB:1GH0"
FT HELIX 126..139
FT /evidence="ECO:0007829|PDB:1GH0"
FT HELIX 144..160
FT /evidence="ECO:0007829|PDB:1GH0"
SQ SEQUENCE 162 AA; 17602 MW; DA87ED20CBD2C354 CRC64;
MKTPLTEAVS IADSQGRFLS STEIQVAFGR FRQAKAGLEA AKALTSKADS LISGAAQAVY
NKFPYTTQMQ GPNYAADQRG KDKCARDIGY YLRMVTYCLI AGGTGPMDEY LIAGIDEINR
TFELSPSWYI EALKYIKANH GLSGDAATEA NSYLDYAINA LS
