ID D8FWG3_9CYAN Unreviewed; 284 AA.
AC D8FWG3;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Cyanophycinase {ECO:0000256|ARBA:ARBA00015719, ECO:0000256|PIRNR:PIRNR032067};
DE EC=3.4.15.6 {ECO:0000256|ARBA:ARBA00013115, ECO:0000256|PIRNR:PIRNR032067};
GN ORFNames=OSCI_1020009 {ECO:0000313|EMBL:CBN54703.1};
OS Kamptonema sp. PCC 6506.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Kamptonema.
OX NCBI_TaxID=272129 {ECO:0000313|EMBL:CBN54703.1, ECO:0000313|Proteomes:UP000004532};
RN [1] {ECO:0000313|Proteomes:UP000004532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6506 {ECO:0000313|Proteomes:UP000004532};
RX PubMed=20675499; DOI=10.1128/JB.00704-10;
RA Mejean A., Mazmouz R., Mann S., Calteau A., Medigue C., Ploux O.;
RT "The genome sequence of the cyanobacterium Oscillatoria sp. PCC 6506
RT reveals several gene clusters responsible for the biosynthesis of toxins
RT and secondary metabolites.";
RL J. Bacteriol. 192:5264-5265(2010).
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:0000256|ARBA:ARBA00002039, ECO:0000256|PIRNR:PIRNR032067}.
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:0000256|ARBA:ARBA00001092,
CC ECO:0000256|PIRNR:PIRNR032067};
CC -!- SIMILARITY: Belongs to the peptidase S51 family.
CC {ECO:0000256|ARBA:ARBA00006534, ECO:0000256|PIRNR:PIRNR032067}.
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DR EMBL; CACA01000099; CBN54703.1; -; Genomic_DNA.
DR RefSeq; WP_007353928.1; NZ_CACA01000099.1.
DR AlphaFoldDB; D8FWG3; -.
DR OrthoDB; 9799980at2; -.
DR Proteomes; UP000004532; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03145; GAT1_cyanophycinase; 1.
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 NCBIfam; TIGR02069; cyanophycinase; 1.
DR PANTHER; PTHR36175; CYANOPHYCINASE; 1.
DR PANTHER; PTHR36175:SF1; CYANOPHYCINASE; 1.
DR Pfam; PF03575; Peptidase_S51; 1.
DR PIRSF; PIRSF032067; Cyanophycinase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR032067};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR032067};
KW Reference proteome {ECO:0000313|Proteomes:UP000004532};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR032067}.
FT ACT_SITE 132
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR032067-1"
FT ACT_SITE 174
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR032067-1"
FT ACT_SITE 201
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR032067-1"
SQ SEQUENCE 284 AA; 30561 MW; CEB20582B10C0E72 CRC64;
MTLSENGGQL LIIGGAEDKE GECKILREFV RRAGGIKARL AIMTAATSLP GEVGDNYIRI
FERLGAEDVR VVDTQRREDA NNPDALEVIQ QATGVFFTGG DQSRITSCLK DTELDAAIHQ
RYSEGIIIGG TSAGAAMMPD IMIIEGESET NPRVDVVAMG PGMGFLPGVV IDQHFAQRGR
LGRLVSALAQ QPAVLGFGID ENTAIAVNGD EFEVIGEGAI TVIDESEKTH DNLDGLLKDE
ALAVCGARLH ILPNGYRFNL KTRKPIFTQQ SQQSEEAREV APAR
//
