ID A0A1I0ZFA5_9CLOT Unreviewed; 276 AA.
AC A0A1I0ZFA5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Cyanophycinase {ECO:0000256|ARBA:ARBA00015719};
DE EC=3.4.15.6 {ECO:0000256|ARBA:ARBA00013115};
GN ORFNames=SAMN04488528_102048 {ECO:0000313|EMBL:SFB24305.1};
OS Clostridium frigidicarnis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=84698 {ECO:0000313|EMBL:SFB24305.1, ECO:0000313|Proteomes:UP000198619};
RN [1] {ECO:0000313|EMBL:SFB24305.1, ECO:0000313|Proteomes:UP000198619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12271 {ECO:0000313|EMBL:SFB24305.1,
RC ECO:0000313|Proteomes:UP000198619};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOKI01000020; SFB24305.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0ZFA5; -.
DR STRING; 84698.SAMN04488528_102048; -.
DR OrthoDB; 9799980at2; -.
DR Proteomes; UP000198619; 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:UP000198619};
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 276 AA; 30023 MW; F47019C54423B21F CRC64;
MKEIIKGKLI IIGGAEDKEG NKEILKIVRD SIDKNTGELV IATIATTNPK EAGDKYNELF
SNLGVKNISI LDVQSREEAH REEKISLVKN AKLIFFTGGD QLRITSIVGG TPLHKELKDA
YSKGCIFAGT SAGASVMSST MVVNGDDEES PKKCTLKMAP GLGLIDRVII DQHFAQRGRI
GRLLGGVAEN PDVLGIGIDE DTAIIVDNDG KFTIMGSGAV YVIDGSCISY SNVSEQNQDE
VLSMFNVKMH ILKEGNNFNL LTRKPLEEER LNNENN
//
