CPHA_TRIV2
ID CPHA_TRIV2 Reviewed; 901 AA.
AC O86109; Q3MC50;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=Ava_1814;
OS Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX NCBI_TaxID=240292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-9; 157-169;
RP 317-327; 602-616; 633-644 AND 829-840, AND SUBUNIT.
RX PubMed=9652408; DOI=10.1046/j.1432-1327.1998.2540154.x;
RA Ziegler K., Diener A., Herpin C., Richter R., Deutzmann R., Lockau W.;
RT "Molecular characterization of cyanophycin synthetase, the enzyme
RT catalyzing the biosynthesis of the cyanobacterial reserve material multi-L-
RT arginyl-poly-L-aspartate (cyanophycin).";
RL Eur. J. Biochem. 254:154-159(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29413 / PCC 7937;
RX PubMed=25197444; DOI=10.4056/sigs.3899418;
RA Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL Stand. Genomic Sci. 9:562-573(2014).
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 -!- 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:0000269|PubMed:9652408}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MurCDEF family.
CC {ECO:0000305}.
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DR EMBL; AJ005201; CAA06440.1; -; Genomic_DNA.
DR EMBL; CP000117; ABA21436.1; -; Genomic_DNA.
DR AlphaFoldDB; O86109; -.
DR SMR; O86109; -.
DR STRING; 240292.Ava_1814; -.
DR EnsemblBacteria; ABA21436; ABA21436; Ava_1814.
DR KEGG; ava:Ava_1814; -.
DR eggNOG; COG0189; Bacteria.
DR eggNOG; COG0769; Bacteria.
DR HOGENOM; CLU_016806_0_0_3; -.
DR OMA; PFMIANA; -.
DR BRENDA; 6.3.2.29; 322.
DR BRENDA; 6.3.2.30; 322.
DR Proteomes; UP000002533; 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 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Ligase; Nucleotide-binding.
FT CHAIN 1..901
FT /note="Cyanophycin synthetase"
FT /id="PRO_0000101712"
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; 98266 MW; 806DCB352C9A67B7 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 RSTIAELIEE INQDPNRGDG HDKVLTKIEL
DRTSYQLLER AGYTLNSVPP KGTICYLRAT ANLSTGGTAV DRTDEIHPEN IWLAQRVVKI
IGLDIAGLDI VTTDISRPLR ELDGVIVEVN AAPGFRMHVA PSQGIPRNVA GAVMDMLFPN
EQSGRIPILS VTGTNGKTTT TRLLAHIYKQ TGKVVGYTTT DGTYIGDYLV ESGDNTGPQS
AHVILQDPTV EVAVLETARG GILRSGLGFE SANVGVVLNV AADHLGIGDI DTIDQLANLK
SVVAESVYPD GYAVLNADDR RVAAMAEKTK ANIAYFTMNP DSELVRKHIQ KGGVAAVYEN
GYLSIVKGDW THRIERAEQI PLTMGGRAPF MIANALAASL AAFVQNVSIE QIRAGLRTFR
ASVSQTPGRM NLFNLGNYHA LVDYAHNPAS YEAVGAFVRN WTSGQRIGVV GGPGDRRDED
FVTLGKLAAE IFDYIIVKED DDTRGRPRGS ASALITKGIT QVKPDARYES ILDETQAINK
GLDMAPANGL VVILPESVSR AIKLIKLRGL VKEEIQQQNP STTVIDNQNG VASSSVINTL
L
