ID K9U2H5_CHRTP Unreviewed; 897 AA.
AC K9U2H5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
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 ORFNames=Chro_3358 {ECO:0000313|EMBL:AFY88818.1};
OS Chroococcidiopsis thermalis (strain PCC 7203).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Chroococcidiopsidales;
OC Chroococcidiopsidaceae; Chroococcidiopsis.
OX NCBI_TaxID=251229 {ECO:0000313|EMBL:AFY88818.1, ECO:0000313|Proteomes:UP000010384};
RN [1] {ECO:0000313|EMBL:AFY88818.1, ECO:0000313|Proteomes:UP000010384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7203 {ECO:0000313|EMBL:AFY88818.1,
RC ECO:0000313|Proteomes:UP000010384};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Chroococcidiopsis thermalis PCC 7203.";
RL Submitted (JUN-2012) 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) + 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; CP003597; AFY88818.1; -; Genomic_DNA.
DR RefSeq; WP_015155363.1; NC_019695.1.
DR AlphaFoldDB; K9U2H5; -.
DR STRING; 251229.Chro_3358; -.
DR KEGG; cthe:Chro_3358; -.
DR PATRIC; fig|251229.3.peg.3917; -.
DR eggNOG; COG0189; Bacteria.
DR eggNOG; COG0769; Bacteria.
DR HOGENOM; CLU_016806_0_0_3; -.
DR InParanoid; K9U2H5; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000010384; 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:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
DR GO; GO:0009059; P:macromolecule biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
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; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR011810; Cya_phycin_syn.
DR InterPro; IPR044019; Cyanophycin_syn_N.
DR InterPro; IPR018109; Folylpolyglutamate_synth_CS.
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.
DR PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 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:UP000010384}.
FT DOMAIN 224..478
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 897 AA; 97305 MW; 0EEBF68DBFE1213B CRC64;
MRILKIQTLR GPNYWSIRRH KLILMRLDLE ELAEQPTNQI PGFYEGLVET LPSLESHFCS
PGCRGGFLMR VREGTMMGHV VEHIALELQE LAGMSVGFGR TRETSTPGIY QVVFDYEDEQ
AGRYAGRAAV RMCQSIVEQG RYPQAELEQD LQDLKELYRD AALGPSTEAI IEEAAAKGIP
WMNLGARFLI QLGYGANQKR VQATMSDRTG ILGVELACDK ESTKRILGNA GVPVPQGTTI
SYLDELEDAI ASVGGYPIVI KPLDGNHGRG ITIDIRTWEE AEAAYDAAKE VSRAVIVERY
YVGRDHRVLV VDGKVVAVAE RVPAHVVGDG ESTIEQLIEE TNQDPNRGEG HDNVLTKIQL
DRTSFQLLER QGYTLDTVLT EGEVCYLRAT ANLSTGGIAV DRTDDIHPEN AWLAQRVAKI
VGLDITGIDI VTSDISRPLR ETEGVIVEVN AAPGFRMHVA PSRGIPRNVA GAVLDMLFPP
GTPSRIPIIA LTGTNGKTTT TRLTAHLIKQ SGKVVGYTTT DGTYIGDYLV EPGDNTGPQS
AQLILQDPTV EVAVLESARG GILRSGLAFD ASDIGVVLNV AADHLGIGDI DTLEQMAHLK
SVVAEAVQPN GYAVLNADDP LTAQMRDRVK SKLAWFSMSP DNPLIQEHTQ QGGLAAVYEN
GYLSILQGDW TLRIEQAANV PLTMGGRAPF MIANALAASL AAYAYGVQIE QIRAGLATFR
ASSSQTPGRM NLFNLGEYHA LVDYAHNPHS YEALGGFIRN WTAGERIGVI GGPGDRRDED
FIMLGRLSAE IFDRIIIKED DDNRGRPRGD AAELISKGIM QVKSDCRYEI VLDETTAINT
GLDTASNGSL VAILPESVSR AISLIQARNP LSDNSLQPPS VAAQDNAMGI VSSVNQI
//
