ID A0A964BT26_9CYAN Unreviewed; 871 AA.
AC A0A964BT26;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 18-JUN-2025, entry version 9.
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:MCC0178629.1};
GN ORFNames=I4641_16775 {ECO:0000313|EMBL:MCC0178629.1};
OS Waterburya agarophytonicola KI4.
OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Pleurocapsales;
OC Hyellaceae; Waterburya; Waterburya agarophytonicola.
OX NCBI_TaxID=2874699 {ECO:0000313|EMBL:MCC0178629.1, ECO:0000313|Proteomes:UP000729733};
RN [1] {ECO:0000313|EMBL:MCC0178629.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KI4 {ECO:0000313|EMBL:MCC0178629.1};
RX PubMed=34674103;
RA Bonthond G., Shalygin S., Bayer T., Weinberger F.;
RT "Draft genome and description of Waterburya agarophytonicola gen. nov. sp.
RT nov. (Pleurocapsales, Cyanobacteria): a seaweed symbiont.";
RL Antonie Van Leeuwenhoek 0:0-0(2021).
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:MCC0178629.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JADWDC010000049; MCC0178629.1; -; Genomic_DNA.
DR RefSeq; WP_229641730.1; NZ_JADWDC010000049.1.
DR Proteomes; UP000729733; Unassembled WGS sequence.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; IPR013651; ATP-grasp_RimK-type.
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; PF18921; Cyanophycin_syn; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR Pfam; PF08443; RimK; 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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:MCC0178629.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000729733}.
FT DOMAIN 224..480
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 871 AA; 94599 MW; 3AC0B2135B41A20E CRC64;
MRILKTQTLR GPNYWSIRRN KLILMLLDLE ELTEKPSNEL AGFYDGLAQV LPSLIEHQCS
RGYRGGFLER VKEGTLMGHI VEHVALELQE LAGMPVGFGR TRETSTPGVF NVVFEYVEEQ
AGRYAGRAAV RLCKSVVETG TYPARELEQD LTDLKELCAN TALGPSTETI IKEAEARKIP
WMWLSARAML QLGHGANQKR IQATLSNNTS ILAVELACDK EGTKTILENA GVPVPQGTVI
EYLDDLEQAI ADIGGYPIVI KPLDGNHGRG ITININDPSE AETAYDLASK SSKSRSVIVE
RYYQGNDHRV LVIDNKVVAV AERVPAHVTG DGQSTVKELI EITNQDPKRG DGHDNVLTKI
TIDPTSKAVL AKQGYDLGSI LPLGTVAYLR ATANLSTGGV AIDRTDEIHP ENLWLAQRVA
KVIGLDIAGI DIVTSDISKP LRETKGVIVE VNAAPGFRMH AAPSEGLPRN VGASVLEMLF
PNNAPSSIPI VAITGTNGKT TTTRLTAHIY RQTGKIVGFT ATDGIYIQEY LVEKGDNTGP
YSAGAILRDP TVEVAVLETA RGGILRSGLA FDSCDIGVVL NVAADHLGLG GIDTIEQMAR
LKGVIAETVK PGGYAILNAD DPLVAAMAAK VSCKVAYFSM NPDNPIVSEH IRRNGLAAIY
ENGYLSILEG KWTLRIEKAV NIPMTMRGMA PFMIANALAS CLATFAQGVD IEEIRRGLRT
FEVSSEQIPG RMNLFDLGEY HALVDYAHNP HGYLAVGDFV KNWQGNRIGV VGGPGDRRDE
DLILLGNISA RIFDSILIKE DEDSRGRKPG EVADLISKGI CQENPNINYE IILDETEAIN
TALDRAKNNN LVVVFPDKIA QAIKLIKQRL N
//
