ID A0A1S9AI30_9BURK Unreviewed; 876 AA.
AC A0A1S9AI30;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Cyanophycin synthetase {ECO:0000256|ARBA:ARBA00022036};
DE EC=6.3.2.29 {ECO:0000256|ARBA:ARBA00013005};
DE EC=6.3.2.30 {ECO:0000256|ARBA:ARBA00012968};
DE AltName: Full=Cyanophycin synthase {ECO:0000256|ARBA:ARBA00031353};
GN ORFNames=B0920_06930 {ECO:0000313|EMBL:OON63134.1};
OS Massilia sp. KIM.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1955422 {ECO:0000313|EMBL:OON63134.1, ECO:0000313|Proteomes:UP000190838};
RN [1] {ECO:0000313|EMBL:OON63134.1, ECO:0000313|Proteomes:UP000190838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM {ECO:0000313|EMBL:OON63134.1,
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: Catalyzes the ATP-dependent polymerization of arginine and
CC aspartate to multi-L-arginyl-poly-L-aspartic acid (cyanophycin; a
CC water-insoluble reserve polymer). {ECO:0000256|ARBA:ARBA00003184}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[L-4-(L-arginin-2-N-yl)aspartate](n) + ATP + L-aspartate = [L-
CC 4-(L-arginin-2-N-yl)aspartate](n)-L-aspartate + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:13277, Rhea:RHEA-COMP:13728, Rhea:RHEA-
CC COMP:13733, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:137986, ChEBI:CHEBI:137990,
CC ChEBI:CHEBI:456216; EC=6.3.2.29;
CC Evidence={ECO:0000256|ARBA:ARBA00000535};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[L-4-(L-arginin-2-N-yl)aspartate](n)-L-aspartate + ATP + L-
CC arginine = [L-4-(L-arginin-2-N-yl)aspartate](n+1) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:23888, Rhea:RHEA-COMP:13732, Rhea:RHEA-
CC COMP:13733, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:137986, ChEBI:CHEBI:137990,
CC ChEBI:CHEBI:456216; EC=6.3.2.30;
CC Evidence={ECO:0000256|ARBA:ARBA00000917};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MurCDEF family.
CC {ECO:0000256|ARBA:ARBA00009060}.
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:OON63134.1}.
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DR EMBL; MVAD01000001; OON63134.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9AI30; -.
DR STRING; 1955422.B0920_06930; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000190838; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0071161; F:cyanophycin synthetase activity (L-arginine-adding); IEA:UniProtKB-EC.
DR GO; GO:0071160; F:cyanophycin synthetase activity (L-aspartate-adding); IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0009059; P:macromolecule biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR011810; Cya_phycin_syn.
DR InterPro; IPR044019; Cyanophycin_syn_N.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR004101; Mur_ligase_C.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp.
DR NCBIfam; TIGR02068; cya_phycin_syn; 1.
DR PANTHER; PTHR23135:SF18; CYANOPHYCIN SYNTHETASE; 1.
DR PANTHER; PTHR23135; MUR LIGASE FAMILY MEMBER; 1.
DR Pfam; PF18921; Cyanophycin_syn; 1.
DR Pfam; PF01071; GARS_A; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SMART; SM01209; GARS_A; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000190838}.
FT DOMAIN 221..474
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 876 AA; 92717 MW; 0E23718C6DB9860A CRC64;
MQILEQRFLR GPNVHADSPC LLTLLDLEDL YGRSTKDIPG FNEALLALLP SLHGQLLPTG
QPGGFAQRLR EGTYLGRVIE HLTLDLQTQA GAPASYGRTR PVAGEPGQFR IVCAYSLEKL
VQPAFQLALD IVDALAHGES IEVEERLEEL REIAGRYAIG TSTAAVLAAA HERGIPTQRI
TEDANLFLLG WGVKQKRLQA TTTGDTSFIA VKIASDKQLT KALLKEAGVP VPEGETVTTV
EAAQRVAARL RAPVTLKPLD ANQGKGVTVN CATPEDVARA FEFARQYGRR IIVERFIEGR
DYRVLVAGGK VSAASCRRPA HVVGDGVSTI RQLVEVENRN PARGEGHTNI LTQIALDAHA
ADMLARQGYE FDSVPPEGAV AELRGNANLS TGGTAEDVTD LLPESTRLLC VRAAAKIGLD
VAGIDIVCKD ISQPLAAQRG AVIEINAAPG IRMHQYPSGG APRDAGEAIV EGLMGDSDGR
IPLVAVTGTN GKTTTTLLIA HAVRLAGHTT GVTTTEGVFI DGKQIVKGDC TGYWSARTVL
SDPTVEFAVL ETARGGLLKR GLAFDRCDVG VVLNVAADHL GLDGIETIED LAQVKALVAL
SATRAAVLNA EDALCVAMAR RVKPGAEVIF FSMDAENPVL LKHLADGGRG VYLQDGAVIV
ADGHSHQALV KVESMPVSFN GAARFNIANS LAAAAALMAS NMGNLQIAAG LSTFVSNGRT
NPLRTNMFDV RGVTVFVDYA HNAAAYAAMA DMARAMLPRQ LVGIVTAPGD RRDEDLRQIG
EVCGARFDEL VVYESQSRGR AVGAAVDLIL EGAQAAVGMS DTLHREIEVG KAVRLGLSLC
EPGDVLVFAT GASLDVFIEA VRVMDPECAD EIAAQV
//
