ID   CPHA_SYNY3              Reviewed;         873 AA.
AC   P73833;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Cyanophycin synthetase;
DE            EC=6.3.2.29;
DE            EC=6.3.2.30;
DE   AltName: Full=Cyanophycin synthase;
GN   Name=cphA; OrderedLocusNames=slr2002;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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:0000250}.
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   -!- 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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the MurCDEF family.
CC       {ECO:0000305}.
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DR   EMBL; BA000022; BAA17890.1; -; Genomic_DNA.
DR   PIR; S75028; S75028.
DR   AlphaFoldDB; P73833; -.
DR   SMR; P73833; -.
DR   STRING; 1148.1652973; -.
DR   PaxDb; P73833; -.
DR   EnsemblBacteria; BAA17890; BAA17890; BAA17890.
DR   KEGG; syn:slr2002; -.
DR   eggNOG; COG0189; Bacteria.
DR   eggNOG; COG0769; Bacteria.
DR   InParanoid; P73833; -.
DR   OMA; PFMIANA; -.
DR   BRENDA; 6.3.2.29; 382.
DR   BRENDA; 6.3.2.30; 382.
DR   SABIO-RK; P73833; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 3.40.1190.10; -; 1.
DR   Gene3D; 3.90.190.20; -; 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   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; SSF53244; SSF53244; 1.
DR   SUPFAM; SSF53623; SSF53623; 1.
DR   TIGRFAMs; TIGR02068; cya_phycin_syn; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..873
FT                   /note="Cyanophycin synthetase"
FT                   /id="PRO_0000101714"
FT   DOMAIN          224..480
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         495..501
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
SQ   SEQUENCE   873 AA;  94695 MW;  EE3C34EAE174A4E8 CRC64;
     MKILKTLTLR GPNYWSIRRK KLIVMRLDLE DLAERPSNSI PGFYEGLIRV LPSLVEHFCS
     PGHRGGFLAR VREGTYMGHI VEHVALELQE LVGMTAGFGR TRETSTPGIY NVVYEYVDEQ
     AGRYAGRAAV RLCRSLVDTG DYSLTELEKD LEDLRDLGAN SALGPSTETI VTEADARKIP
     WMLLSARAMV QLGYGVHQQR IQATLSSHSG ILGVELACDK EGTKTILQDA GIPVPRGTTI
     QYFDDLEEAI NDVGGYPVVI KPLDGNHGRG ITINVRHWEE AIAAYDLAAE ESKSRSIIVE
     RYYEGSDHRV LVVNGKLVAV AERIPAHVTG DGTSTITELI DKTNQDPNRG DGHANILTKI
     VVNKTAIDVM ERQGYNLDSV LPKDEVVYLR ATANLSTGGI AIDRTDDIHP ENIWLMERVA
     KVIGLDIAGI DVVTSDISKP LRETNGVIVE VNAAPGFRMH VAPSQGLPRN VAAPVLDMLF
     PSGTPSRIPI LAVTGTNGKT TTTRLLAHIY RQTGKTVGYT STDAIYINEY CVEKGDNTGP
     QSAAVILRDP TVEVAVLETA RGGILRAGLA FDTCDVGVVL NVAADHLGLG DIDTIEQMAK
     VKSVIAEVVD PSGYAVLNAD DPLVAAMADK VKAKVAYFSM NPDNPVIQNH IRRNGIAAVY
     ESGYVSILEG SWTLRVEEAT LIPMTMGGMA PFMIANALAA CLAAFVNGLD VEVIRQGVRT
     FTTSAEQTPG RMNLFNLGRY HALVDYAHNP AGYRAVGDFV KNWHGQRFGV VGGPGDRRDS
     DLIELGQIAA QVFDRIIVKE DDDKRGRSGG ETADLIVKGI LQENPGAAYE VILDETVALN
     KALDQVEEKG LVVVFPESVS KAIELIKARK PIG