ID   CPCE_NOSS1              Reviewed;         276 AA.
AC   P07125;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Phycocyanobilin lyase subunit alpha;
DE            EC=4.-.-.-;
DE   AltName: Full=Phycocyanin operon protein CpcE;
GN   Name=cpcE; OrderedLocusNames=alr0532;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3109890; DOI=10.1002/j.1460-2075.1987.tb04833.x;
RA   Belknap W.R., Haselkorn R.;
RT   "Cloning and light regulation of expression of the phycocyanin operon of
RT   the cyanobacterium Anabaena.";
RL   EMBO J. 6:871-884(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11237320; DOI=10.1006/abio.2000.4979;
RA   Cai Y.A., Murphy J.T., Wedemayer G.J., Glazer A.N.;
RT   "Recombinant phycobiliproteins. Recombinant C-phycocyanins equipped with
RT   affinity tags, oligomerization, and biospecific recognition domains.";
RL   Anal. Biochem. 290:186-204(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
CC   -!- FUNCTION: Required for the chromophorylation of the CpcA gene product.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: CpcE and CpcF associate to form a lyase. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CpcE/RpcE/PecE family. {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to be a linker peptide.
CC       {ECO:0000305|PubMed:3109890}.
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DR   EMBL; X05239; CAA28866.1; -; Genomic_DNA.
DR   EMBL; AF178757; AAG09320.1; -; Genomic_DNA.
DR   EMBL; BA000019; BAB72490.1; -; Genomic_DNA.
DR   PIR; AC1873; AC1873.
DR   RefSeq; WP_010994708.1; NZ_RSCN01000059.1.
DR   PDB; 5N3U; X-ray; 1.89 A; A=1-276.
DR   PDBsum; 5N3U; -.
DR   AlphaFoldDB; P07125; -.
DR   SMR; P07125; -.
DR   STRING; 103690.17129877; -.
DR   PRIDE; P07125; -.
DR   EnsemblBacteria; BAB72490; BAB72490; BAB72490.
DR   KEGG; ana:alr0532; -.
DR   eggNOG; COG1413; Bacteria.
DR   OMA; AWWLGKF; -.
DR   OrthoDB; 1138269at2; -.
DR   BRENDA; 4.4.1.32; 8113.
DR   Proteomes; UP000002483; Chromosome.
DR   GO; GO:0030089; C:phycobilisome; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.10.10; -; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR004155; PBS_lyase_HEAT.
DR   Pfam; PF03130; HEAT_PBS; 2.
DR   SMART; SM00567; EZ_HEAT; 6.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antenna complex; Lyase; Phycobilisome; Reference proteome.
FT   CHAIN           1..276
FT                   /note="Phycocyanobilin lyase subunit alpha"
FT                   /id="PRO_0000199266"
FT   STRAND          13..15
FT                   /evidence="ECO:0007829|PDB:5N3U"
FT   HELIX           19..25
FT                   /evidence="ECO:0007829|PDB:5N3U"
FT   HELIX           31..43
FT                   /evidence="ECO:0007829|PDB:5N3U"
FT   HELIX           49..58
FT                   /evidence="ECO:0007829|PDB:5N3U"
FT   HELIX           67..69
FT                   /evidence="ECO:0007829|PDB:5N3U"
FT   HELIX           72..83
FT                   /evidence="ECO:0007829|PDB:5N3U"
FT   HELIX           87..89
FT                   /evidence="ECO:0007829|PDB:5N3U"
FT   HELIX           90..96
FT                   /evidence="ECO:0007829|PDB:5N3U"
FT   HELIX           102..115
FT                   /evidence="ECO:0007829|PDB:5N3U"
FT   HELIX           118..120
FT                   /evidence="ECO:0007829|PDB:5N3U"
FT   HELIX           121..126
FT                   /evidence="ECO:0007829|PDB:5N3U"
FT   TURN            127..131
FT                   /evidence="ECO:0007829|PDB:5N3U"
FT   HELIX           132..134
FT                   /evidence="ECO:0007829|PDB:5N3U"
FT   HELIX           148..157
FT                   /evidence="ECO:0007829|PDB:5N3U"
FT   HELIX           161..163
FT                   /evidence="ECO:0007829|PDB:5N3U"
FT   HELIX           164..167
FT                   /evidence="ECO:0007829|PDB:5N3U"
FT   HELIX           168..172
FT                   /evidence="ECO:0007829|PDB:5N3U"
FT   HELIX           176..190
FT                   /evidence="ECO:0007829|PDB:5N3U"
FT   HELIX           193..203
FT                   /evidence="ECO:0007829|PDB:5N3U"
FT   HELIX           208..221
FT                   /evidence="ECO:0007829|PDB:5N3U"
FT   HELIX           224..226
FT                   /evidence="ECO:0007829|PDB:5N3U"
FT   HELIX           227..232
FT                   /evidence="ECO:0007829|PDB:5N3U"
FT   STRAND          233..235
FT                   /evidence="ECO:0007829|PDB:5N3U"
FT   HELIX           237..250
FT                   /evidence="ECO:0007829|PDB:5N3U"
FT   HELIX           263..273
FT                   /evidence="ECO:0007829|PDB:5N3U"
SQ   SEQUENCE   276 AA;  29628 MW;  2B557E79B97159CF CRC64;
     MIEPSVEEFP AENGPQLTPE LAIANLQSSD LSLRYYAAWW LGKYRVKESA AVDALIAALE
     DEADRTELGG YPLRRNAARA LGKLGNRKAV PGLINCLECP DFYVREAAAQ SLEMLKDKTA
     APALIKLLDG GVAQAVQVTG RPHLVQPYEA VLEALGAIGA TDAIPLIQPF LEHPVSRVQC
     AAARAMYQLT QEPVYGELLV KVLAGNDLNL RRVALGDLGA IGYLAAAEAI ANAKAENSFK
     LIALKGLLEH QMSAESNALS ISDQAIRVMN LMDSLL