PHEA1_CHRS2
ID PHEA1_CHRS2 Reviewed; 132 AA.
AC U5T880;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Phycocyanin PC645 alpha-1 subunit {ECO:0000305};
DE Short=PC645A1 {ECO:0000303|PubMed:24979784};
OS Chroomonas sp. (strain CCMP270).
OG Plastid; Chloroplast {ECO:0000312|EMBL:AGY96990.1}.
OC Eukaryota; Cryptophyceae; Pyrenomonadales; Chroomonadaceae; Chroomonas;
OC unclassified Chroomonas.
OX NCBI_TaxID=354589;
RN [1] {ECO:0000312|EMBL:AGY96990.1, ECO:0007744|PDB:4LMS}
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF
RP 53-132 IN COMPLEX WITH 15,16-DIHYDROBILIVERDIN; MESOBILIVERDIN AND
RP PHYCOCYANOBILIN, 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 phycoerythrin family. {ECO:0000305}.
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DR EMBL; KF314693; AGY96990.1; -; mRNA.
DR PDB; 4LMS; X-ray; 1.35 A; A=53-132.
DR PDBsum; 4LMS; -.
DR SMR; U5T880; -.
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; 3.90.510.10; -; 1.
DR InterPro; IPR011070; Globular_prot_asu/bsu.
DR InterPro; IPR037011; Phycoerythr-like_a_sf.
DR InterPro; IPR004228; Phycoerythr_a.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF02972; Phycoerythr_ab; 1.
DR SUPFAM; SSF56568; SSF56568; 1.
DR PROSITE; PS51318; TAT; 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..132
FT /note="Phycocyanin PC645 alpha-1 subunit"
FT /id="PRO_5004664466"
FT BINDING 54
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="1"
FT /ligand_note="ligand shared with beta subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMS"
FT BINDING 68
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="2"
FT /ligand_note="ligand shared with beta subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMS"
FT BINDING 70
FT /ligand="mesobiliverdin"
FT /ligand_id="ChEBI:CHEBI:189061"
FT /ligand_note="ligand shared with beta subunit"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMS"
FT BINDING 76
FT /ligand="mesobiliverdin"
FT /ligand_id="ChEBI:CHEBI:189061"
FT /ligand_note="ligand shared with beta subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMS"
FT BINDING 77
FT /ligand="mesobiliverdin"
FT /ligand_id="ChEBI:CHEBI:189061"
FT /ligand_note="ligand shared with beta subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMS"
FT BINDING 92
FT /ligand="mesobiliverdin"
FT /ligand_id="ChEBI:CHEBI:189061"
FT /ligand_note="ligand shared with beta subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMS"
FT BINDING 123
FT /ligand="15,16-dihydrobiliverdin"
FT /ligand_id="ChEBI:CHEBI:57899"
FT /ligand_note="ligand shared with beta subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMS"
FT BINDING 125
FT /ligand="15,16-dihydrobiliverdin"
FT /ligand_id="ChEBI:CHEBI:57899"
FT /ligand_note="ligand shared with beta subunit"
FT /evidence="ECO:0000269|PubMed:24979784,
FT ECO:0007744|PDB:4LMS"
SQ SEQUENCE 132 AA; 13725 MW; D16ED216CCAC0F82 CRC64;
MIAKTVAVLA LAGSAAAYAP TMSLSANRRE LVQGAAAAAV VAPLLRPTGA SARDAQLRAP
IVEIFDARGC DAKNAQYTGP KSNDMNDDQC VKVSMQKITV SEATAAKKLQ EFIGGKATAI
NVPIISSMTK KY
