ID   PHEA_MASLA              Reviewed;         162 AA.
AC   P00309;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Phycoerythrocyanin alpha chain;
GN   Name=pccA;
OS   Mastigocladus laminosus (Fischerella sp.).
OC   Bacteria; Cyanobacteria; Nostocales; Hapalosiphonaceae; Mastigocladus.
OX   NCBI_TaxID=83541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2121619; DOI=10.1016/0378-1119(90)90480-f;
RA   Eberlein M., Kufer W.;
RT   "Genes encoding both subunits of phycoerythrocyanin, a light-harvesting
RT   biliprotein from the cyanobacterium Mastigocladus laminosus.";
RL   Gene 94:133-136(1990).
RN   [2]
RP   PROTEIN SEQUENCE.
RX   PubMed=6411579; DOI=10.1515/bchm2.1983.364.1.691;
RA   Fueglistaller P., Suter F., Zuber H.;
RT   "The complete amino-acid sequence of both subunits of phycoerythrocyanin
RT   from the thermophilic cyanobacterium Mastigocladus laminosus.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 364:691-712(1983).
RN   [3]
RP   CHROMOPHORE STRUCTURE, AND CHROMOPHORE BINDING AT CYS-84.
RA   Bishop J.E., Rapoport H., Klotz A.V., Chan C.F., Glazer A.N.,
RA   Fueglistaller P., Zuber H.;
RT   "Chromopeptides from phycoerythrocyanin. Structure and linkage of the three
RT   bilin groups.";
RL   J. Am. Chem. Soc. 109:875-881(1987).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX   PubMed=2106585; DOI=10.1016/0022-2836(90)90270-v;
RA   Duerring M., Huber R., Bode W., Ruembelli R., Zuber H.;
RT   "Refined three-dimensional structure of phycoerythrocyanin from the
RT   cyanobacterium Mastigocladus laminosus at 2.7 A.";
RL   J. Mol. Biol. 211:633-644(1990).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-162, AND CHROMOPHORE BINDING AT
RP   CYS-84.
RX   PubMed=17209552; DOI=10.1021/bi061844j;
RA   Schmidt M., Patel A., Zhao Y., Reuter W.;
RT   "Structural basis for the photochemistry of alpha-phycoerythrocyanin.";
RL   Biochemistry 46:416-423(2007).
CC   -!- FUNCTION: Light-harvesting photosynthetic bile pigment-protein from the
CC       phycobiliprotein complex.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=~550 nm;
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane
CC       protein; Cytoplasmic side. Note=Forms the periphery of the
CC       phycobilisome rod.
CC   -!- PTM: Contains one covalently linked bilin chromophore.
CC   -!- SIMILARITY: Belongs to the phycobiliprotein family. {ECO:0000305}.
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DR   EMBL; M34254; AAC64654.1; -; Genomic_DNA.
DR   PDB; 2C7J; X-ray; 3.00 A; A=1-162.
DR   PDB; 2C7K; X-ray; 3.20 A; A=1-162.
DR   PDB; 2C7L; X-ray; 2.85 A; A=1-162.
DR   PDB; 2J96; X-ray; 2.25 A; A/B=1-162.
DR   PDBsum; 2C7J; -.
DR   PDBsum; 2C7K; -.
DR   PDBsum; 2C7L; -.
DR   PDBsum; 2J96; -.
DR   AlphaFoldDB; P00309; -.
DR   SMR; P00309; -.
DR   EvolutionaryTrace; P00309; -.
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   Pfam; PF00502; Phycobilisome; 1.
DR   PIRSF; PIRSF000081; Phycocyanin; 1.
DR   SUPFAM; SSF46458; SSF46458; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antenna complex; Bile pigment; Chromophore;
KW   Direct protein sequencing; Electron transport; Membrane; Photosynthesis;
KW   Phycobilisome; Thylakoid; Transport.
FT   CHAIN           1..162
FT                   /note="Phycoerythrocyanin alpha chain"
FT                   /id="PRO_0000199169"
FT   BINDING         84
FT                   /ligand="(15Z)-phycoviolobilin"
FT                   /ligand_id="ChEBI:CHEBI:189063"
FT                   /note="covalent, via 1 link"
FT   HELIX           4..15
FT                   /evidence="ECO:0007829|PDB:2J96"
FT   TURN            21..24
FT                   /evidence="ECO:0007829|PDB:2J96"
FT   HELIX           25..28
FT                   /evidence="ECO:0007829|PDB:2J96"
FT   HELIX           31..62
FT                   /evidence="ECO:0007829|PDB:2J96"
FT   HELIX           64..66
FT                   /evidence="ECO:0007829|PDB:2J96"
FT   STRAND          71..74
FT                   /evidence="ECO:0007829|PDB:2J96"
FT   HELIX           78..101
FT                   /evidence="ECO:0007829|PDB:2J96"
FT   HELIX           105..110
FT                   /evidence="ECO:0007829|PDB:2J96"
FT   TURN            111..114
FT                   /evidence="ECO:0007829|PDB:2J96"
FT   HELIX           115..118
FT                   /evidence="ECO:0007829|PDB:2J96"
FT   TURN            119..122
FT                   /evidence="ECO:0007829|PDB:2J96"
FT   HELIX           126..138
FT                   /evidence="ECO:0007829|PDB:2J96"
FT   HELIX           144..160
FT                   /evidence="ECO:0007829|PDB:2J96"
SQ   SEQUENCE   162 AA;  17564 MW;  C069332836F2BD2E CRC64;
     MKTPLTEAIA AADLRGSYLS NTELQAVFGR FNRARAGLEA ARAFANNGKK WAEAAANHVY
     QKFPYTTQMQ GPQYASTPEG KAKCVRDIDH YLRTISYCCV VGGTGPLDDY VVAGLKEFNS
     ALGLSPSWYI AALEFVRDNH GLTGDVAGEA NTYINYAINA LS