ID K9YKY0_CYASC Unreviewed; 873 AA.
AC K9YKY0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
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 OrderedLocusNames=Cyast_1640 {ECO:0000313|EMBL:AFZ47601.1};
OS Cyanobacterium stanieri (strain ATCC 29140 / PCC 7202).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Geminocystaceae; Cyanobacterium.
OX NCBI_TaxID=292563 {ECO:0000313|EMBL:AFZ47601.1, ECO:0000313|Proteomes:UP000010483};
RN [1] {ECO:0000313|Proteomes:UP000010483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29140 / PCC 7202 {ECO:0000313|Proteomes:UP000010483};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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}.
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DR EMBL; CP003940; AFZ47601.1; -; Genomic_DNA.
DR AlphaFoldDB; K9YKY0; -.
DR STRING; 292563.Cyast_1640; -.
DR KEGG; csn:Cyast_1640; -.
DR PATRIC; fig|292563.3.peg.1712; -.
DR eggNOG; COG0769; Bacteria.
DR eggNOG; COG1181; Bacteria.
DR HOGENOM; CLU_016806_0_0_3; -.
DR BioCyc; CSTA292563:G1353-1650-MONOMER; -.
DR Proteomes; UP000010483; Chromosome.
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; 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 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|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000010483}.
FT DOMAIN 224..480
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 873 AA; 95315 MW; 9D673732AFDF910E CRC64;
MKILKTQTLR GPNYWSIRRQ KLIQMRLDLE DVAEKPSNEI PGFYEGLVEI LPTLIEHFCS
RDHRGGFLER VKEGTYMGHI IEHIALELQE LAGMPVGFGR TRETSTPGVY NVVFEYVYEE
AGRYAGRAAV RLCNSIIKTG SYPPQELAQD IADLNDLRAT SALGPSTETI IKEAETRSIP
WMMLSARSMV QLGYGVNQRR IQATLSEHSG ILGVELACDK EGTKTILRDA GVPVPRGTVI
YYLDELADAI EDVGGYPIVI KPLDGNHGRG ITIDINDWED AEDAYDLAAA ASKTRSVIVE
KYYQGNDHRL LVINGKLIAV SERVPAHVVG DGTSTIDELI EQTNSDPNRG DGHDNVLTRI
SIDRTSLSVL KRQGFDMDTV LKEGEIAYLR ATANLSTGGI AIDRTDDIHP KNVWIAERTA
KIIGLDIAGI DVVTPDITKP LDEVDGVIVE VNAAPGFRMH VAPSQGLPRN VAAPVLEMLY
PDNQPSRIPI LAVTGTNGKT TTTRLLAHIY RQTGKVVGYT STDGIYLGEY MVEKGDNTGP
LSAGVILKDP TVEVAVLECA RGGMLRSGLA FDSCDVGVVL NVAADHLGLG DIDTIEQMAR
VKGIIAEAVN PDGYSILNAD DPLVAQMAKN VKGKVAYFSM SENNPIIIDH LRRDGIAAIY
ENGYLSIFEG EWTLRIEKAE NIPVTMKGMA PFMIANALAA SLAAFVNGVD IELIRQGVRT
FNPGAAQTPG RMNLFEIKDY SVLVDYAHNP AGYEAVGAFV KNWQGDRLGV IGGPGDRRDE
DLMLLGKIAA QTFDHIIVKE DDDKRGREKG EAADLIVKGI LSENPEASYN VIIDEMEALE
TGLEKVKPKG LVVIFPESVT RTIEFIEKTQ QDG
//
