ID A0A0M2TZR3_9FIRM Unreviewed; 269 AA.
AC A0A0M2TZR3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Cyanophycinase {ECO:0000256|ARBA:ARBA00015719};
DE EC=3.4.15.6 {ECO:0000256|ARBA:ARBA00013115};
GN ORFNames=SY88_19290 {ECO:0000313|EMBL:KKM09316.1};
OS Clostridiales bacterium PH28_bin88.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=1605376 {ECO:0000313|EMBL:KKM09316.1, ECO:0000313|Proteomes:UP000034222};
RN [1] {ECO:0000313|EMBL:KKM09316.1, ECO:0000313|Proteomes:UP000034222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Robbins S., Tyson G.;
RT "High quality genome sequence of Candidatus Suratobacter aromatica.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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 -!- SIMILARITY: Belongs to the peptidase S51 family.
CC {ECO:0000256|ARBA:ARBA00006534}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKM09316.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LAKY01000066; KKM09316.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2TZR3; -.
DR STRING; 1605376.SY88_19290; -.
DR PATRIC; fig|1605376.3.peg.3358; -.
DR Proteomes; UP000034222; 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};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000034222};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT ACT_SITE 131
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR032067-1"
FT ACT_SITE 173
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR032067-1"
FT ACT_SITE 200
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR032067-1"
SQ SEQUENCE 269 AA; 28635 MW; 5845C4B03777B30E CRC64;
MGDQVQGTLV IIGGAEDKEH ECEILKKVVE LSGGVKARLV VMTAATERPQ AVGNEYRRIF
SRLGVKDITI TDISSREEAN HPRHVAAIQS ASAIFFTGGD QLRITSLLGG TEVDRALHVS
YRKGVVIAGT SAGASVMSET MIVEGNSEEA PKKNTLKMAP GMGLIAEVVV DQHFAQRGRL
GRLLTAVAQN PHMLGLGLDE DTAVVVGTDD CFEVYGSQTV TVVDGTAISH TNVSESAPAQ
ALALTDVRLH VLPAGYRFNL KQRQPLIPG
//