PHCB1_MICDP
ID PHCB1_MICDP Reviewed; 172 AA.
AC P07119;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=C-phycocyanin-1 beta subunit;
GN Name=cpcB1;
OS Microchaete diplosiphon (Fremyella diplosiphon).
OC Bacteria; Cyanobacteria; Nostocales; Rivulariaceae; Microchaete.
OX NCBI_TaxID=1197;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Mazel D., Houmard J., Tandeau de Marsac N.;
RT "A multigene family in Calothrix sp. PCC 7601 encodes phycocyanin, the
RT major component of the cyanobacterial light harvesting antenna.";
RL Mol. Gen. Genet. 211:296-304(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3127591; DOI=10.1016/0022-2836(88)90617-1;
RA Conley P.B., Lemaux P.G., Grossman A.;
RT "Molecular characterization and evolution of sequences encoding light-
RT harvesting components in the chromatically adapting cyanobacterium
RT Fremyella diplosiphon.";
RL J. Mol. Biol. 199:447-465(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 158-172.
RX PubMed=3086870; DOI=10.1073/pnas.83.11.3924;
RA Conley P.B., Lemaux P.G., Lomax T.L., Grossman A.R.;
RT "Genes encoding major light-harvesting polypeptides are clustered on the
RT genome of the cyanobacterium Fremyella diplosiphon.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:3924-3928(1986).
RN [4] {ECO:0007744|PDB:1CPC}
RP X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) IN COMPLEX WITH PHYCOCYANOBILIN
RP CHROMOPHORE, SUBUNIT, AND METHYLATION AT ASN-72.
RX PubMed=1899708; DOI=10.1016/0022-2836(91)90759-y;
RA Duerring M., Schmidt G.B., Huber R.;
RT "Isolation, crystallization, crystal structure analysis and refinement of
RT constitutive C-phycocyanin from the chromatically adapting cyanobacterium
RT Fremyella diplosiphon at 1.66-A resolution.";
RL J. Mol. Biol. 217:577-592(1991).
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: Heterodimer of an alpha and a beta subunit, which further
CC assembles into trimers and the trimers into hexamers.
CC {ECO:0000269|PubMed:1899708}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane
CC protein; Cytoplasmic side. Note=Part of the phycobilisome rod.
CC -!- INDUCTION: Phycocyanin-1 is expressed at similar levels in green and
CC red light (constitutive phycocyanin).
CC -!- PTM: Contains two covalently linked bilin chromophores.
CC {ECO:0000269|PubMed:1899708, ECO:0007744|PDB:1CPC}.
CC -!- SIMILARITY: Belongs to the phycobiliprotein family. {ECO:0000305}.
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DR EMBL; X06084; CAA29464.1; -; Genomic_DNA.
DR EMBL; X07013; CAA30064.1; -; Genomic_DNA.
DR EMBL; M13218; AAA24878.1; -; Genomic_DNA.
DR PIR; S00713; S00713.
DR PDB; 1CPC; X-ray; 1.66 A; B/L=1-172.
DR PDBsum; 1CPC; -.
DR AlphaFoldDB; P07119; -.
DR SMR; P07119; -.
DR iPTMnet; P07119; -.
DR PRIDE; P07119; -.
DR EvolutionaryTrace; P07119; -.
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; IPR006247; Phycocyanin_b.
DR Pfam; PF00502; Phycobilisome; 1.
DR PIRSF; PIRSF000081; Phycocyanin; 1.
DR SUPFAM; SSF46458; SSF46458; 1.
DR TIGRFAMs; TIGR01339; phycocy_beta; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antenna complex; Bile pigment; Chromophore;
KW Electron transport; Membrane; Methylation; Photosynthesis; Phycobilisome;
KW Thylakoid; Transport.
FT CHAIN 1..172
FT /note="C-phycocyanin-1 beta subunit"
FT /id="PRO_0000199145"
FT BINDING 82
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="1"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000269|PubMed:1899708,
FT ECO:0007744|PDB:1CPC"
FT BINDING 153
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="2"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000269|PubMed:1899708,
FT ECO:0007744|PDB:1CPC"
FT MOD_RES 72
FT /note="N4-methylasparagine"
FT /evidence="ECO:0000269|PubMed:1899708,
FT ECO:0007744|PDB:1CPC"
FT CONFLICT 4
FT /note="A -> T (in Ref. 2; CAA30064)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="Q -> H (in Ref. 2; CAA30064)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="I -> N (in Ref. 2; CAA30064)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="S -> T (in Ref. 2; CAA30064)"
FT /evidence="ECO:0000305"
FT HELIX 4..13
FT /evidence="ECO:0007829|PDB:1CPC"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:1CPC"
FT HELIX 21..32
FT /evidence="ECO:0007829|PDB:1CPC"
FT HELIX 34..46
FT /evidence="ECO:0007829|PDB:1CPC"
FT HELIX 48..62
FT /evidence="ECO:0007829|PDB:1CPC"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:1CPC"
FT HELIX 76..99
FT /evidence="ECO:0007829|PDB:1CPC"
FT HELIX 103..108
FT /evidence="ECO:0007829|PDB:1CPC"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:1CPC"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:1CPC"
FT HELIX 124..142
FT /evidence="ECO:0007829|PDB:1CPC"
FT HELIX 154..171
FT /evidence="ECO:0007829|PDB:1CPC"
SQ SEQUENCE 172 AA; 17920 MW; 5C0E56C521F0DE1F CRC64;
MLDAFAKVVS QADARGEYLS GSQIDALSAL VADGNKRMDV VNRITGNSST IVANAARSLF
AEQPQLIAPG GNAYTSRRMA ACLRDMEIIL RYVTYAIFAG DASVLDDRCL NGLKETYLAL
GTPGSSVAVG VQKMKDAALA IAGDTNGITR GDCASLMAEV ASYFDKAASA VA
