CPCS1_NOSS1
ID CPCS1_NOSS1 Reviewed; 188 AA.
AC Q8YZ70;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Phycocyanobilin lyase CpcS 1;
DE EC=4.-.-.-;
DE AltName: Full=Phycocyanobilin:Cys-beta84-phycobiliprotein lyase CpcS;
DE AltName: Full=Phycocyanobilin:Cys-beta84-phycobiliprotein lyase CpcS-III;
DE AltName: Full=Phycocyanobilin:Cys-beta84-phycobiliprotein lyase CpeS;
GN Name=cpcS1; Synonyms=cpeS1; OrderedLocusNames=alr0617;
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 [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).
RN [2]
RP FUNCTION AS A PHYCOCYANOBILIN LYASE PROTEIN, SUBUNIT, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND ACTIVITY REGULATION.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=16452471; DOI=10.1074/jbc.m513796200;
RA Zhao K.H., Su P., Li J., Tu J.M., Zhou M., Bubenzer C., Scheer H.;
RT "Chromophore attachment to phycobiliprotein beta-subunits:
RT phycocyanobilin:cysteine-beta84 phycobiliprotein lyase activity of CpeS-
RT like protein from Anabaena Sp. PCC7120.";
RL J. Biol. Chem. 281:8573-8581(2006).
RN [3]
RP FUNCTION AS A CHROMOPHORE LYASE, AND INDUCTION.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=17895251; DOI=10.1074/jbc.m703038200;
RA Zhao K.H., Zhang J., Tu J.M., Bohm S., Ploscher M., Eichacker L.,
RA Bubenzer C., Scheer H., Wang X., Zhou M.;
RT "Lyase activities of CpcS- and CpcT-like proteins from Nostoc PCC7120 and
RT sequential reconstitution of binding sites of phycoerythrocyanin and
RT phycocyanin beta-subunits.";
RL J. Biol. Chem. 282:34093-34103(2007).
RN [4]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND PROTEIN SUBSTRATES.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=17726096; DOI=10.1073/pnas.0706209104;
RA Zhao K.H., Su P., Tu J.M., Wang X., Liu H., Ploscher M., Eichacker L.,
RA Yang B., Zhou M., Scheer H.;
RT "Phycobilin:cystein-84 biliprotein lyase, a near-universal lyase for
RT cysteine-84-binding sites in cyanobacterial phycobiliproteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:14300-14305(2007).
RN [5]
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, REACTION MECHANISM,
RP CHROMOPHORE-BINDING, AND MUTAGENESIS OF 21-HIS-HIS-22; ARG-147 AND ARG-149.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=19864423; DOI=10.1074/jbc.m109.056382;
RA Kupka M., Zhang J., Fu W.L., Tu J.M., Bohm S., Su P., Chen Y., Zhou M.,
RA Scheer H., Zhao K.H.;
RT "Catalytic mechanism of S-type phycobiliprotein lyase: chaperone-like
RT action and functional amino acid residues.";
RL J. Biol. Chem. 284:36405-36414(2009).
CC -!- FUNCTION: Catalyzes the site-selective attachment of phycocyanobilin
CC (PCB) to 'Cys-82' in CpcB and 'Cys-83' in PecB. Also able to add PCB to
CC ApcA1, ApcA2, ApcB, ApcD and ApcF, but not PecA. In vitro can be made
CC to add phycoerythrobilin, a non-physiological substrate, to its target
CC proteins (using genes from Fremyella diplosiphon PCC 7601). Binds PCB
CC extremely rapidly, followed by a much slower phase of PCB transfer to
CC the apo-acceptor protein. This suggests that the lyase has a chaperone-
CC like function, and may serve to regulate the manner (possibly the
CC conformation) in which the chromophore is attached to its target rather
CC than to accelerate the rate. {ECO:0000269|PubMed:16452471,
CC ECO:0000269|PubMed:17895251}.
CC -!- ACTIVITY REGULATION: Inhibited by Co(2+), Cu(2+), Ni(2+), Zn(2+), beta-
CC mercaptoethanol, and non-competitively by imidazole.
CC {ECO:0000269|PubMed:16452471, ECO:0000269|PubMed:19864423}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.7 uM for ApcA1 {ECO:0000269|PubMed:16452471,
CC ECO:0000269|PubMed:17726096, ECO:0000269|PubMed:19864423};
CC KM=2.4 uM for ApcF {ECO:0000269|PubMed:16452471,
CC ECO:0000269|PubMed:17726096, ECO:0000269|PubMed:19864423};
CC KM=1.14 uM for PCB {ECO:0000269|PubMed:16452471,
CC ECO:0000269|PubMed:17726096, ECO:0000269|PubMed:19864423};
CC pH dependence:
CC Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:16452471,
CC ECO:0000269|PubMed:17726096, ECO:0000269|PubMed:19864423};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:16452471, ECO:0000269|PubMed:17726096,
CC ECO:0000269|PubMed:19864423};
CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:16452471}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:17895251}.
CC -!- SIMILARITY: Belongs to the CpcS/CpeS biliprotein lyase family.
CC {ECO:0000305}.
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DR EMBL; BA000019; BAB72575.1; -; Genomic_DNA.
DR PIR; AH1883; AH1883.
DR RefSeq; WP_010994793.1; NZ_RSCN01000009.1.
DR AlphaFoldDB; Q8YZ70; -.
DR SMR; Q8YZ70; -.
DR STRING; 103690.17129963; -.
DR EnsemblBacteria; BAB72575; BAB72575; BAB72575.
DR KEGG; ana:alr0617; -.
DR eggNOG; ENOG502Z8E6; Bacteria.
DR OMA; LWFASPN; -.
DR OrthoDB; 1672344at2; -.
DR BioCyc; MetaCyc:MON-18986; -.
DR BRENDA; 4.4.1.29; 319.
DR Proteomes; UP000002483; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0017009; P:protein-phycocyanobilin linkage; IDA:UniProtKB.
DR Gene3D; 2.40.128.20; -; 1.
DR HAMAP; MF_01459; Chrphore_lyase_CpxS; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR018536; CpcS/CpeS.
DR Pfam; PF09367; CpeS; 1.
PE 1: Evidence at protein level;
KW Lyase; Reference proteome.
FT CHAIN 1..188
FT /note="Phycocyanobilin lyase CpcS 1"
FT /id="PRO_0000403136"
FT MUTAGEN 21..22
FT /note="HH->TV: Reduced lyase activity, reduced binding of
FT PCB."
FT /evidence="ECO:0000269|PubMed:19864423"
FT MUTAGEN 147
FT /note="R->Q: Reduced lyase activity, reduced binding of
FT PCB."
FT /evidence="ECO:0000269|PubMed:19864423"
FT MUTAGEN 149
FT /note="R->L: Loss of catalytic activity, retains PCB
FT binding."
FT /evidence="ECO:0000269|PubMed:19864423"
SQ SEQUENCE 188 AA; 20704 MW; 563E30FE3D319831 CRC64;
MNIEEFFELS AGKWFSHRTS HHLAFKQSED GKSDLVIESL AADHPEVIKL CELYEVPASA
ASCGARVSWN GTMEWDEEKH TGSTVLATVP DVDNPNEGRL LREMGYAEKA PVAGRYKMGD
DGALTLTTEY ETMWSEERLW FASPNLRMRV SVLKRFGGFS MASFTSEIRM GGSPAAAKAE
EAANSASS
