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PHEA2_CHRS2
ID   PHEA2_CHRS2             Reviewed;         122 AA.
AC   U5T8W5;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   22-JAN-2014, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Phycocyanin PC645 alpha-2 subunit {ECO:0000305};
DE            Short=PC645A2 {ECO:0000303|PubMed:24979784};
OS   Chroomonas sp. (strain CCMP270).
OG   Plastid; Chloroplast {ECO:0000312|EMBL:AGY96992.1}.
OC   Eukaryota; Cryptophyceae; Pyrenomonadales; Chroomonadaceae; Chroomonas;
OC   unclassified Chroomonas.
OX   NCBI_TaxID=354589;
RN   [1] {ECO:0000312|EMBL:AGY96992.1, ECO:0007744|PDB:4LMS}
RP   NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF
RP   53-132 IN COMPLEX WITH MESOBILIVERDIN AND 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 and one mesobiliverdin
CC       chromophore with binding 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; KF314695; AGY96992.1; -; mRNA.
DR   PDB; 4LMS; X-ray; 1.35 A; C=53-122.
DR   PDBsum; 4LMS; -.
DR   SMR; U5T8W5; -.
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   Pfam; PF02972; Phycoerythr_ab; 1.
DR   SUPFAM; SSF56568; SSF56568; 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..122
FT                   /note="Phycocyanin PC645 alpha-2 subunit"
FT                   /id="PRO_5004664575"
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"
SQ   SEQUENCE   122 AA;  12640 MW;  B584018F2E0B2082 CRC64;
     MIAKTVAILA LAGSAAAYAP TMSLSANRRE LVQGAAAAAV VAPMLRPTGA SAKDAQLRAP
     VVTIFDARGC KDHANKEYTD PKAGNAENDE CCVKVQMTPI KVADDAAALV LKECLSELKG
     KK
 
 
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