ID A0A1Z4NJ78_9CYAN Unreviewed; 287 AA.
AC A0A1Z4NJ78;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=NIES3974_24410 {ECO:0000313|EMBL:BAZ05786.1};
OS Calothrix sp. NIES-3974.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=2005462 {ECO:0000313|EMBL:BAZ05786.1, ECO:0000313|Proteomes:UP000218621};
RN [1] {ECO:0000313|EMBL:BAZ05786.1, ECO:0000313|Proteomes:UP000218621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-3974 {ECO:0000313|EMBL:BAZ05786.1,
RC ECO:0000313|Proteomes:UP000218621};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) 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, 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; AP018254; BAZ05786.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4NJ78; -.
DR OrthoDB; 9799980at2; -.
DR Proteomes; UP000218621; Chromosome.
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:UP000218621};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR032067}.
FT ACT_SITE 144
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR032067-1"
FT ACT_SITE 186
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR032067-1"
FT ACT_SITE 213
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR032067-1"
SQ SEQUENCE 287 AA; 31584 MW; A68372CFAD6C128E CRC64;
MQQLKAKWLE MRTPQATKTA VLVIGGAEDK VHGREILRTF VARSGGTDAY ITIIPSASRE
PGIIGGRYIR IFEEMGAQKV ELLDIRERDQ CEDRHFRESL ENCTGLFLTG GDQLRLCGVL
SDTSAMEIIR HRVKTGQLTL AGTSAGAAVM GHHMIAGGGS GESPNRSLVD MATGLGFIPE
VIVDQHFHNR NRMVRLVSAI AAHPDRLGIG IDEDTCAMFE RDGWMQVLGK GSVTVVDPTE
VTHTNEPHVG ATEPLTIHNM RLHILSHGDR YHLYQRTVLP ATYRISS
//
