CPHA_GEMHP
ID CPHA_GEMHP Reviewed; 874 AA.
AC P56947;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 78.
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;
OS Geminocystis herdmanii (strain PCC 6308) (Synechocystis sp. (strain PCC
OS 6308)).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Chroococcaceae; Geminocystis.
OX NCBI_TaxID=113355;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11131019; DOI=10.1007/s002030000206;
RA Aboulmagd E., Oppermann-Sanio F.B., Steinbuechel A.;
RT "Molecular characterization of the cyanophycin synthetase from
RT Synechocystis sp. strain PCC6308.";
RL Arch. Microbiol. 174:297-306(2000).
RN [2]
RP SEQUENCE REVISION TO 52-60.
RA Aboulmagd E., Oppermann-Sanio F.B., Steinbuechel A.;
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=11319097; DOI=10.1128/aem.67.5.2176-2182.2001;
RA Aboulmagd E., Oppermann-Sanio F.B., Steinbuechel A.;
RT "Purification of Synechocystis sp. strain PCC6308 cyanophycin synthetase
RT and its characterization with respect to substrate and primer
RT specificity.";
RL Appl. Environ. Microbiol. 67:2176-2182(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).
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:0000269|PubMed:11319097};
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:0000269|PubMed:11319097};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=450 mM for L-aspartic acid {ECO:0000269|PubMed:11319097};
CC KM=49 mM for L-arginine {ECO:0000269|PubMed:11319097};
CC KM=200 mM for ATP {ECO:0000269|PubMed:11319097};
CC pH dependence:
CC Optimum pH is 8.2. {ECO:0000269|PubMed:11319097};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:11319097};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:11319097}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MurCDEF family.
CC {ECO:0000305}.
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DR EMBL; AF220099; AAF43647.2; -; Genomic_DNA.
DR AlphaFoldDB; P56947; -.
DR SMR; P56947; -.
DR PRIDE; P56947; -.
DR BioCyc; MetaCyc:MON-17423; -.
DR BRENDA; 6.3.2.29; 382.
DR BRENDA; 6.3.2.30; 382.
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 1: Evidence at protein level;
KW ATP-binding; Ligase; Nucleotide-binding.
FT CHAIN 1..874
FT /note="Cyanophycin synthetase"
FT /id="PRO_0000101715"
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 874 AA; 95031 MW; A8ACE565E485A93F CRC64;
MKILKTQTLR GPNYWSIRRQ KLIQMRLDLE DVAEKPSNLI PGFYEGLVKI LPSLVEHFCS
RDHRGGFLER VQEGTYMGHI VEHIALELQE LAGMPVGFGR TRETSTPGIY NVVFEYVYEE
AGRYAGRVAV RLCNSIITTG AYGLDELAQD LSDLKDLRAN SALGPSTETI IKEAEARQIP
WMLLSARAMV QLGYGANQQR IQATLSNKTG ILGVELACDK EGTKTTLAEA GIPVPRGTVI
YYADELADAI ADVGGYPIVL KPLDGNHGRG ITIDINSQQE AEEAYDLASA ASKTRSVIVE
RYYKGNDHRV LVINGKLVAV SERIPAHVTG NGSSTIEELI QETNEHPDRG DGHDNVLTRI
SIDRTSLGVL KRQGFEMDTV LKKGEVAYLR ATANLSTGGI AIDRTDEIHP QNIWIAERVA
KIIGLDIAGI DVVTPDITKP LTEVDGVIVE VNAAPGFRMH VAPSQGLPRN VAAPVIDMLF
PDNHPSRIPI LAVTGTNGKT TTTRLLAHIY RQTGKVVGYT STDGIYLGDY MVEKGDNTGP
VSAGVILRDP TVEVAVLECA RGGILRSGLA FESCDVGVVL NVAEDHLGLG DIDTIEQMAK
VKGVIAESVN ADGYAVLNAD DPLVAQMAKN VKGKIAYFSM SKDNPIIIDH LRRNGMAAVY
ENGYLSIFEG EWTLRIEKAE NIPVTMKAMA PFMIANALAA SLAAFVHGID IELIRQGVRS
FNPGANQTPG RMNLFDMKDF SVLIDYAHNP AGYLAVGSFV KNWKGDRLGV IGGPGDRRDE
DLMLLGKIAS QIFDHIIIKE DDDNRGRDRG TVADLIAKGI VAENPNASYD DILDETEAIE
TGLKKVDKGG LVVIFPESVT GSIEMIEKYH LSSE
