ID A0A4Z0C1W1_9BURK Unreviewed; 858 AA.
AC A0A4Z0C1W1;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 18-JUN-2025, entry version 19.
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 Name=cphA {ECO:0000313|EMBL:TFZ04480.1};
GN ORFNames=EZ242_01645 {ECO:0000313|EMBL:TFZ04480.1};
OS Ramlibacter rhizophilus.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=1781167 {ECO:0000313|EMBL:TFZ04480.1, ECO:0000313|Proteomes:UP000297564};
RN [1] {ECO:0000313|EMBL:TFZ04480.1, ECO:0000313|Proteomes:UP000297564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC AB2015357 {ECO:0000313|EMBL:TFZ04480.1,
RC ECO:0000313|Proteomes:UP000297564};
RA Zhang X., Feng G., Zhu H.;
RT "Ramlibacter rhizophilus CCTCC AB2015357, whole genome shotgun sequence.";
RL Submitted (MAR-2019) 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) + L-aspartate + ATP = [L-
CC 4-(L-arginin-2-N-yl)aspartate](n)-L-aspartate + ADP + phosphate +
CC H(+); 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:ARBA00048425};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[L-4-(L-arginin-2-N-yl)aspartate](n)-L-aspartate + L-arginine
CC + ATP = [L-4-(L-arginin-2-N-yl)aspartate](n+1) + ADP + phosphate +
CC H(+); 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:ARBA00048094};
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:TFZ04480.1}.
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DR EMBL; SMLL01000001; TFZ04480.1; -; Genomic_DNA.
DR RefSeq; WP_135283362.1; NZ_SMLL01000001.1.
DR AlphaFoldDB; A0A4Z0C1W1; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000297564; 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:UniProtKB-KW.
DR GO; GO:0009058; P: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; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
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 NCBIfam; TIGR02068; cya_phycin_syn; 1.
DR NCBIfam; NF010623; PRK14016.1; 1.
DR PANTHER; PTHR23135:SF18; CYANOPHYCIN SYNTHETASE; 1.
DR PANTHER; PTHR23135; MUR LIGASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF18921; Cyanophycin_syn; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 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 Ligase {ECO:0000313|EMBL:TFZ04480.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000297564}.
FT DOMAIN 207..459
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 858 AA; 91156 MW; 7DC563E6F54D8449 CRC64;
MEISRIRALR GPNLWSRHTS IEAIVACAPD DIAVTDRPEF ESRLRKLFPA IGALRGPGPM
SLAHVLEAAA LALQEEAGCP VTFSRTQATA DAGVFQVVVE YSEEAVGRLA FELARQLVAA
TLDPQAGFDV DSALARLREI DEDLRLGPST GSIVQAAVAR GVPFQRLTEG SLVQFGWGKH
QRRIWAAEVD QTSAVSESIA QDKELSKRLL RSVGVPVPAG RPVADEADAW AAALEVGLPV
VVKPRDGNQG KGITVNVNTR EGMALAYKAA VEIGEVMVEK YLRGSDHRLL VVGDQLVAAA
RREPPVVVGD GECTVAELVA KVNADPRRGD GHATSLTKIR IDDIAIALLA EQGLRIDSVP
ARGQRVPMRH NANLSTGGTA TDVTDDVHPE VAERAIAAAQ MVGLHVCGVD MVCESVLAPL
EEQGGGIVEV NAAPGLRMHL SPSYGKPRNV GEAIVAHMFE PGHDGRVPVV AVTGVNGKTT
TVRLIAHLFA GSGLKVGMTN TDGVYVDGRQ IDSGDCSGPK SARSVLMHPD VEAAVFETAR
GGILREGLGF DHCRVAVVTN VGSGDHLGLN HIHTVEELAV LKRVIVQNVT PREGYAVLNA
ADPLVAAMAA VCPGKVIYFA TERQHAVMTA HRAQGGRVVY VDPALEGGSV VACEGNWRRH
VRLADIPITR NGTIGFQVEN VMAAIGGAWG AGLAWDAIRS GLATFVSDAH TVPGRFNVMD
WRGATVIADY GHNPDAMRVL VCAVEAMPAR RRSVVISAAG DRRDQDIREQ TAILGAAFDD
VLLYQDAAQR GRADGQVMAL LRDGLQGASR ATRVEEIRGE FLAVDTALAR LQPGDLCLVL
VDQVEEALAH LARRMAEG
//
