CPHB_SYNY3
ID CPHB_SYNY3 Reviewed; 271 AA.
AC P73832;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Cyanophycinase;
DE EC=3.4.15.6;
GN Name=cphB; OrderedLocusNames=slr2001;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP PROTEIN SEQUENCE OF 2-16, CLEAVAGE OF INITIATOR METHIONINE, FUNCTION,
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10429200; DOI=10.1046/j.1432-1327.1999.00479.x;
RA Richter R., Hejazi M., Kraft R., Ziegler K., Lockau W.;
RT "Cyanophycinase, a peptidase degrading the cyanobacterial reserve material
RT multi-L-arginyl-poly-L-aspartic acid (cyanophycin): molecular cloning of
RT the gene of Synechocystis sp. PCC 6803, expression in Escherichia coli, and
RT biochemical characterization of the purified enzyme.";
RL Eur. J. Biochem. 263:163-169(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF APOPROTEIN, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITES, AND
RP MUTAGENESIS OF ASP-17; ASP-100; GLN-101; SER-132; ASP-158; ASP-172;
RP GLN-173; ARG-178; ARG-180; ARG-183 AND ASP-202.
RX PubMed=19591842; DOI=10.1016/j.jmb.2009.07.001;
RA Law A.M., Lai S.W., Tavares J., Kimber M.S.;
RT "The structural basis of beta-peptide-specific cleavage by the serine
RT protease cyanophycinase.";
RL J. Mol. Biol. 392:393-404(2009).
CC -!- FUNCTION: Exopeptidase that catalyzes the hydrolytic cleavage of multi-
CC L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve
CC polymer) into aspartate-arginine dipeptides.
CC {ECO:0000269|PubMed:10429200, ECO:0000269|PubMed:19591842}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[L-4-(L-arginin-2-N-yl)aspartate](n) + H2O = [L-4-(L-arginin-
CC 2-N-yl)aspartate](n-1) + L-4-(L-arginin-2-N-yl)aspartate;
CC Xref=Rhea:RHEA:12845, Rhea:RHEA-COMP:13728, Rhea:RHEA-COMP:13734,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:137986, ChEBI:CHEBI:137991;
CC EC=3.4.15.6; Evidence={ECO:0000269|PubMed:10429200,
CC ECO:0000269|PubMed:19591842};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.2 uM for cyanophycin (at 30 degrees Celsius and pH 8.0)
CC {ECO:0000269|PubMed:10429200, ECO:0000269|PubMed:19591842};
CC Note=kcat is 16.5 sec(-1) for cyanophycin.;
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:10429200,
CC ECO:0000269|PubMed:19591842};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:10429200, ECO:0000269|PubMed:19591842};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19591842}.
CC -!- SIMILARITY: Belongs to the peptidase S51 family. {ECO:0000305}.
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DR EMBL; BA000022; BAA17889.1; -; Genomic_DNA.
DR PIR; S75027; S75027.
DR PDB; 3EN0; X-ray; 1.50 A; A/B/C=1-271.
DR PDBsum; 3EN0; -.
DR AlphaFoldDB; P73832; -.
DR SMR; P73832; -.
DR IntAct; P73832; 1.
DR STRING; 1148.1652972; -.
DR MEROPS; S51.003; -.
DR PaxDb; P73832; -.
DR EnsemblBacteria; BAA17889; BAA17889; BAA17889.
DR KEGG; syn:slr2001; -.
DR eggNOG; COG4242; Bacteria.
DR InParanoid; P73832; -.
DR OMA; FMTGGDQ; -.
DR PhylomeDB; P73832; -.
DR BioCyc; MetaCyc:MON-17422; -.
DR BRENDA; 3.4.15.6; 382.
DR EvolutionaryTrace; P73832; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0008236; F:serine-type peptidase activity; IDA:UniProtKB.
DR GO; GO:0044260; P:cellular macromolecule metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR005320; Peptidase_S51.
DR InterPro; IPR011811; Peptidase_S51_cyanophycinase.
DR Pfam; PF03575; Peptidase_S51; 1.
DR PIRSF; PIRSF032067; Cyanophycinase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR02069; cyanophycinase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Protease;
KW Reference proteome; Serine protease.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10429200"
FT CHAIN 2..271
FT /note="Cyanophycinase"
FT /id="PRO_0000209974"
FT ACT_SITE 132
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:19591842"
FT ACT_SITE 174
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:19591842"
FT ACT_SITE 201
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:19591842"
FT MUTAGEN 17
FT /note="D->A: 1.7-fold decrease in enzyme activity."
FT /evidence="ECO:0000269|PubMed:19591842"
FT MUTAGEN 100
FT /note="D->A: 2.5-fold decrease in enzyme activity."
FT /evidence="ECO:0000269|PubMed:19591842"
FT MUTAGEN 101
FT /note="Q->A: 5000-fold decrease in enzyme activity."
FT /evidence="ECO:0000269|PubMed:19591842"
FT MUTAGEN 132
FT /note="S->A: 50000-fold decrease in enzyme activity."
FT /evidence="ECO:0000269|PubMed:19591842"
FT MUTAGEN 158
FT /note="D->A: 2.4-fold decrease in enzyme activity."
FT /evidence="ECO:0000269|PubMed:19591842"
FT MUTAGEN 172
FT /note="D->A: 5000-fold decrease in enzyme activity."
FT /evidence="ECO:0000269|PubMed:19591842"
FT MUTAGEN 173
FT /note="Q->A: 200-fold decrease in enzyme activity."
FT /evidence="ECO:0000269|PubMed:19591842"
FT MUTAGEN 178
FT /note="R->A: 100-fold decrease in enzyme activity."
FT /evidence="ECO:0000269|PubMed:19591842"
FT MUTAGEN 180
FT /note="R->A: 10000-fold decrease in enzyme activity."
FT /evidence="ECO:0000269|PubMed:19591842"
FT MUTAGEN 183
FT /note="R->A: 10000-fold decrease in enzyme activity."
FT /evidence="ECO:0000269|PubMed:19591842"
FT MUTAGEN 202
FT /note="D->A: 12.5-fold decrease in enzyme activity."
FT /evidence="ECO:0000269|PubMed:19591842"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:3EN0"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:3EN0"
FT HELIX 23..31
FT /evidence="ECO:0007829|PDB:3EN0"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:3EN0"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:3EN0"
FT HELIX 49..63
FT /evidence="ECO:0007829|PDB:3EN0"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:3EN0"
FT HELIX 76..80
FT /evidence="ECO:0007829|PDB:3EN0"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:3EN0"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:3EN0"
FT HELIX 101..108
FT /evidence="ECO:0007829|PDB:3EN0"
FT HELIX 112..122
FT /evidence="ECO:0007829|PDB:3EN0"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:3EN0"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:3EN0"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:3EN0"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:3EN0"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:3EN0"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:3EN0"
FT TURN 175..180
FT /evidence="ECO:0007829|PDB:3EN0"
FT HELIX 181..190
FT /evidence="ECO:0007829|PDB:3EN0"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:3EN0"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:3EN0"
FT STRAND 211..219
FT /evidence="ECO:0007829|PDB:3EN0"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:3EN0"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:3EN0"
FT STRAND 245..253
FT /evidence="ECO:0007829|PDB:3EN0"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:3EN0"
FT TURN 261..264
FT /evidence="ECO:0007829|PDB:3EN0"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:3EN0"
SQ SEQUENCE 271 AA; 29390 MW; 8D65A50E82E65919 CRC64;
MPLSSQPAIL IIGGAEDKVH GREILQTFWS RSGGNDAIIG IIPSASREPL LIGERYQTIF
SDMGVKELKV LDIRDRAQGD DSGYRLFVEQ CTGIFMTGGD QLRLCGLLAD TPLMDRIRQR
VHNGEISLAG TSAGAAVMGH HMIAGGSSGE WPNRALVDMA VGLGIVPEIV VDQHFHNRNR
MARLLSAIST HPELLGLGID EDTCAMFERD GSVKVIGQGT VSFVDARDMS YTNAALVGAN
APLSLHNLRL NILVHGEVYH QVKQRAFPRV T
