ID   CPHA_NOSS1              Reviewed;         901 AA.
AC   P58572;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=all3879;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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; BA000019; BAB75578.1; -; Genomic_DNA.
DR   PIR; AH2290; AH2290.
DR   RefSeq; WP_010998020.1; NZ_RSCN01000011.1.
DR   AlphaFoldDB; P58572; -.
DR   SMR; P58572; -.
DR   STRING; 103690.17133013; -.
DR   EnsemblBacteria; BAB75578; BAB75578; BAB75578.
DR   KEGG; ana:all3879; -.
DR   eggNOG; COG0189; Bacteria.
DR   eggNOG; COG0769; Bacteria.
DR   OMA; PFMIANA; -.
DR   OrthoDB; 1861122at2; -.
DR   BRENDA; 6.3.2.29; 319.
DR   BRENDA; 6.3.2.30; 319.
DR   Proteomes; UP000002483; 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..901
FT                   /note="Cyanophycin synthetase"
FT                   /id="PRO_0000101711"
FT   DOMAIN          224..478
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         493..499
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
SQ   SEQUENCE   901 AA;  98290 MW;  CB985234A467694F CRC64;
     MRILKIQTLR GPNYWSIRRH KLIVMRLDLE TLAETPSNEI PGFYEGLVEA LPSLEGHYCS
     PGCHGGFLMR VREGTMMGHI VEHVALELQE LAGMHVGFGR TRETATPGIY QVVIEYLNEE
     AGRYAGRAAV RLCQSIVDRG RYPKAELEQD IQDLKDLWRD ASLGPSTEAI VKEAEKRGIP
     WMQLSARFLI QLGYGVNHKR MQATMTDKTG ILGVELACDK EATKRILAAS GVPVPRGTVI
     NFLDDLEEAI EYVGGYPIVI KPLDGNHGRG ITIDIRSWEE AEAAYEAARQ VSRSIIVERY
     YVGRDHRVLV VDGKVVAVAE RVPAHVIGNG RSTVAELIEE INQDPNRGDG HDKVLTKIEL
     DRTSYQLLER AGYTLNSVPP KGTICYLRAT ANLSTGGTAV DRTDEIHPEN VWLAQRVVKI
     IGLDIAGLDI VTTDISRPLR ELDGVIVEVN AAPGFRMHVA PSQGIPRNVA GAVMDMLFPN
     EQSGRIPILS VTGTNGKTTT TRLLAHIYKQ TGKVVGYTTT DGTYIGDYLV ESGDNTGPQS
     AHVILQDPTV EVAVLETARG GILRSGLGFE SANVGVVLNV AADHLGIGDI DTIDQLANLK
     SVVAESVYPD GYAVLNADDR RVAAMAEKTK ANIAYFTMNS ESELVRKHIQ KGGVAAVYEN
     GYLSIVKGDW THRIERAEQI PLTMGGRAPF MIANALAASL AAFVQNVSIE QIRAGLRTFR
     ASVSQTPGRM NLFNLGNYHA LVDYAHNPAS YEAVGAFVRN WTSGQRIGVV GGPGDRRDED
     FVTLGKLAAE IFDYIIVKED DDTRGRPRGS ASELITKGIT QVKPDARYES ILDETQAINK
     GLDMAPANGL VVILPESVSR AIKLIKLRGL VKEEIQQQNS STTVIDNQNG VASSSVINTL
     L