ID A0A085FXM5_9BURK Unreviewed; 291 AA.
AC A0A085FXM5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Cyanophycinase {ECO:0000256|ARBA:ARBA00015719};
DE EC=3.4.15.6 {ECO:0000256|ARBA:ARBA00013115};
GN ORFNames=FG94_00314 {ECO:0000313|EMBL:KFC76220.1};
OS Massilia sp. LC238.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1502852 {ECO:0000313|EMBL:KFC76220.1, ECO:0000313|Proteomes:UP000028601};
RN [1] {ECO:0000313|EMBL:KFC76220.1, ECO:0000313|Proteomes:UP000028601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC238 {ECO:0000313|EMBL:KFC76220.1,
RC ECO:0000313|Proteomes:UP000028601};
RA Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT isolate.";
RL Submitted (JUN-2014) 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:KFC76220.1}.
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DR EMBL; JNNN01000007; KFC76220.1; -; Genomic_DNA.
DR RefSeq; WP_036206080.1; NZ_JNNN01000007.1.
DR AlphaFoldDB; A0A085FXM5; -.
DR STRING; 1502852.FG94_00314; -.
DR PATRIC; fig|1502852.3.peg.306; -.
DR eggNOG; COG4242; Bacteria.
DR OrthoDB; 9799980at2; -.
DR Proteomes; UP000028601; 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 Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT ACT_SITE 134
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR032067-1"
FT ACT_SITE 176
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR032067-1"
FT ACT_SITE 203
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR032067-1"
SQ SEQUENCE 291 AA; 31213 MW; 8D5666281C36B435 CRC64;
MSEQQHKNGH LVIIGGHEDR KREMEILKRF VELSGGEDAN IVVITAASTV ADEMWSIYDE
AFGSLGVEKR RHLEVTSRQD ANSEEFVRQV DEATGIFMTG GDQKRLLALL GGSALDAAMH
VALKVRGATI GGTSAGASAM SGHMLATGRV ELHPEKGSVS LGAGLGFLHR VVIDQHFSER
QRLSRLLSVV AQNPYLQGIG IDEDTALVVD IGVGIEVLGQ GAVTIVDGRT MITNVADIKD
RDTPELIDVR LHLLPAGSSY RLPAADSEGG RGLPPPLLDF LENVTKRNPL S
//