ID A0A1S9A6Z8_9BURK Unreviewed; 402 AA.
AC A0A1S9A6Z8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Cyanophycinase {ECO:0000256|ARBA:ARBA00015719};
DE EC=3.4.15.6 {ECO:0000256|ARBA:ARBA00013115};
GN ORFNames=B0920_22850 {ECO:0000313|EMBL:OON59241.1};
OS Massilia sp. KIM.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1955422 {ECO:0000313|EMBL:OON59241.1, ECO:0000313|Proteomes:UP000190838};
RN [1] {ECO:0000313|EMBL:OON59241.1, ECO:0000313|Proteomes:UP000190838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM {ECO:0000313|EMBL:OON59241.1,
RC ECO:0000313|Proteomes:UP000190838};
RA Vikram S., Kabwe M.H., Bezuidt O., Govender N., Makhalanyane T.P.;
RT "Genome sequence of Massilia sp. KIM isolated from grassland biome soil in
RT South Africa.";
RL Submitted (FEB-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}.
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:OON59241.1}.
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DR EMBL; MVAD01000004; OON59241.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9A6Z8; -.
DR STRING; 1955422.B0920_22850; -.
DR OrthoDB; 9799980at2; -.
DR Proteomes; UP000190838; 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 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:UP000190838};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..402
FT /note="Cyanophycinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010563607"
SQ SEQUENCE 402 AA; 42899 MW; 0CCAA7C7777A9323 CRC64;
MLRKLCFALA VGIASAGGSL AAEAPKGSLV IIGGGLRPDN AAVWGKIVEL AGGKGARIAV
FPSAAENPER EGRMAADYLN RHGARAFVVP VAPRLPGSDA RKAADDPAIA RSVREAGGAF
FTGGDQARIT GTLRRADGSN TAVLDALWAL YRRGGVIAGT SAGAAIMSST MFYDPPLEVA
PVLKNGVTDG KDIAPGLGFI GEDVFIDQHL LARGRFARML PAMLSKGYKL GLGIDENTAA
VVAPSREVSV IGYTGAILLE LDDAVSDKAQ PRFNLSNARI SYLDNGDRFH LASRSFVAGP
GKEPVDATRP EHRDYLFYTD ILGNNAVVSI LAKLVDSDLQ RATGLAFEGP PSPNPERGYE
FTFSRAPDSR QFVTNREDAW SIYRIRMDVR PVRMQQPLYT PE
//
