ID   CPCE_SYNE7              Reviewed;         273 AA.
AC   Q44115; Q31PD5;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 2.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Phycocyanobilin lyase subunit alpha;
DE            EC=4.-.-.-;
DE   AltName: Full=Phycocyanin operon protein CpcE;
GN   Name=cpcE; OrderedLocusNames=Synpcc7942_1054;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7524727; DOI=10.1007/bf00039542;
RA   Bhalerao R.P., Lind L.K., Gustafsson P.;
RT   "Cloning of the cpcE and cpcF genes from Synechococcus sp. PCC 6301 and
RT   their inactivation in Synechococcus sp. PCC 7942.";
RL   Plant Mol. Biol. 26:313-326(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; M94218; AAA64533.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB57084.1; -; Genomic_DNA.
DR   PIR; S52643; S52643.
DR   RefSeq; WP_011242806.1; NC_007604.1.
DR   AlphaFoldDB; Q44115; -.
DR   SMR; Q44115; -.
DR   STRING; 1140.Synpcc7942_1054; -.
DR   PRIDE; Q44115; -.
DR   EnsemblBacteria; ABB57084; ABB57084; Synpcc7942_1054.
DR   KEGG; syf:Synpcc7942_1054; -.
DR   eggNOG; COG1413; Bacteria.
DR   HOGENOM; CLU_1010860_0_0_3; -.
DR   OMA; AWWLGKF; -.
DR   OrthoDB; 1138269at2; -.
DR   BioCyc; MetaCyc:SYNPCC7942_1054-MON; -.
DR   BioCyc; SYNEL:SYNPCC7942_1054-MON; -.
DR   BRENDA; 4.4.1.32; 7781.
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; 1.
DR   SMART; SM00567; EZ_HEAT; 6.
DR   SUPFAM; SSF48371; SSF48371; 2.
PE   3: Inferred from homology;
KW   Antenna complex; Lyase; Phycobilisome.
FT   CHAIN           1..273
FT                   /note="Phycocyanobilin lyase subunit alpha"
FT                   /id="PRO_0000199271"
FT   CONFLICT        207..219
FT                   /note="RSALMDLGAIGYL -> AVGPDGFRGDRLF (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        229
FT                   /note="L -> V (in Ref. 1; AAA64533)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        254..271
FT                   /note="AIAELDESAIALMDLMDG -> RSQSWMSRQSR (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   273 AA;  29511 MW;  EA00852DCBA95630 CRC64;
     MSEAGTPAEA LTYEQAIANL RQTADTGDRY YAAWWLGRFR MKQPEAIALL IEALDDSLDR
     APDGGYPLRR NAARALGKLE SPEAIAPLIA CLQCEDYYVR EAATQSLGEL QATVAVPALL
     KLLEGGPEAI AAIPGKPHLT QPADAVMETL GQLRATVAVP VVQAFLEHPI DKIRLAAARS
     LYQLTGDDHY AERVVQGLSD PKLQRRRSAL MDLGAIGYLP AAPQIAQTLA ENSLKLISLK
     GLLDTHLRQQ TPEAIAELDE SAIALMDLMD GLL