CPHB_TRIV2
ID CPHB_TRIV2 Reviewed; 298 AA.
AC O86108; Q3MC51;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Cyanophycinase;
DE EC=3.4.15.6;
GN Name=cphB; OrderedLocusNames=Ava_1813;
OS Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX NCBI_TaxID=240292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9652408; DOI=10.1046/j.1432-1327.1998.2540154.x;
RA Ziegler K., Diener A., Herpin C., Richter R., Deutzmann R., Lockau W.;
RT "Molecular characterization of cyanophycin synthetase, the enzyme
RT catalyzing the biosynthesis of the cyanobacterial reserve material multi-L-
RT arginyl-poly-L-aspartate (cyanophycin).";
RL Eur. J. Biochem. 254:154-159(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29413 / PCC 7937;
RX PubMed=25197444; DOI=10.4056/sigs.3899418;
RA Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL Stand. Genomic Sci. 9:562-573(2014).
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 -!- 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;
CC -!- SIMILARITY: Belongs to the peptidase S51 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABA21435.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ005201; CAA06439.1; -; Genomic_DNA.
DR EMBL; CP000117; ABA21435.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; O86108; -.
DR SMR; O86108; -.
DR STRING; 240292.Ava_1813; -.
DR EnsemblBacteria; ABA21435; ABA21435; Ava_1813.
DR KEGG; ava:Ava_1813; -.
DR eggNOG; COG4242; Bacteria.
DR HOGENOM; CLU_053928_0_0_3; -.
DR BRENDA; 3.4.15.6; 322.
DR Proteomes; UP000002533; Chromosome.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Hydrolase; Protease; Serine protease.
FT CHAIN 1..298
FT /note="Cyanophycinase"
FT /id="PRO_0000209972"
FT ACT_SITE 155
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 173
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 197
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
SQ SEQUENCE 298 AA; 32391 MW; 9F039C5F8D9C673E CRC64;
MAPKVVDRRN TMPQLQAKSL EMRTPQATKT AVLVIGGAED KVHGREILRT FFGRAGASKA
YITIIPSASR EPAIIGGRYI RIFEEMGAEK VEILDIRERE QCESSQVRAS LEACSGVFLT
GGDQLRLCGV LSDTPVMEII RQRVRGGQLT LAGTSAGAAV MGHHMIAGGG SGETPNRSLV
DMATGLGLIP EVIVDQHFHN RNRMGRLISA VAAHPDRLGI GIDEDTCAVF ERDGWLQVLG
KGSVTIVDPT ELTHTNEPHV GANEPLTVHN LRLHILSYGD RFHLYQRTVL PAVHRISS
