ID A0A254NA08_9BURK Unreviewed; 853 AA.
AC A0A254NA08;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 Name=cphA {ECO:0000313|EMBL:OWR02258.1};
GN ORFNames=CDO81_21230 {ECO:0000313|EMBL:OWR02258.1};
OS Roseateles puraquae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=431059 {ECO:0000313|EMBL:OWR02258.1, ECO:0000313|Proteomes:UP000197446};
RN [1] {ECO:0000313|EMBL:OWR02258.1, ECO:0000313|Proteomes:UP000197446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 52769 {ECO:0000313|EMBL:OWR02258.1,
RC ECO:0000313|Proteomes:UP000197446};
RX PubMed=17978231; DOI=10.1099/ijs.0.65149-0;
RA Gomila M., Bowien B., Falsen E., Moore E.R., Lalucat J.;
RT "Description of Pelomonas aquatica sp. nov. and Pelomonas puraquae sp.
RT nov., isolated from industrial and haemodialysis water.";
RL Int. J. Syst. Evol. Microbiol. 57:2629-2635(2007).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWR02258.1}.
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DR EMBL; NISI01000010; OWR02258.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A254NA08; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000197446; Unassembled WGS sequence.
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; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
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; PF02786; CPSase_L_D2; 1.
DR Pfam; PF18921; Cyanophycin_syn; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 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:UP000197446}.
FT DOMAIN 204..456
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 853 AA; 90888 MW; C8E9AADB4534CC8D CRC64;
MDVSRTRALR GPNMWSRHTA IEAVVHCNDA ERSLERLPGF EARLRQRFPT IGALRADASL
AQVLEQATLA LQAQAGCPVT FSQTHVTPEA GTYQVVVEYS EEDVGRLAFE QAVKLVSAAL
DGSEFDAEPV LAQLRELDED IRLGPSTGSI VNAAVARGIP YRRLTQGSLV QFGWGAKQRR
IWAAEVDATS AVSESIAQDK DLCKRLLQAA GVPVPIGRPV DSPDDGWAVA QEIGLPVVVK
PQDGNQGKGV TVNVVDRAHF DIAYKAADEI GQVMVEKFLP GGDYRLLVIG DKLIAAARRD
PPHVIGDGTH TVKQLVDKVN SDPRRGDGHA TSLTKIRFDD IAVARLTQQG LTPESIPEKG
QRVILRNNAN LSTGGTATDV TDDVHPEVAA RAIAAAQVVG LHVCGVDVVA ESVLRPLEEI
NGGIVEVNAA PGLRMHLSPS FGKGRNVGEA IIGHLFGTGT KAEDGRIPVV AVTGTNGKTT
VTRLIAHMFA SCGLKVGMTN TDGVYVDGRQ IDSGDCSGPK SARNVLMHPD VEAAVLETAR
GGILREGLGF DRCQVAVVTN IGAGDHLGMN FLHTAEDIVL VKRVIVQNVA PNGYAVLNAA
DPLTAQMAAV CPGQVIYFAA DRHHPLMATH RAQGKRCVYV DGDQIVAAQG VWRESIPLRD
IPLTRGGVIG FQVENAMAAV AAAWGVGLDW DTIRRGVGSF ANDADNAPGR FNVMDYRGAT
VIADYGHNGD AMKALVDAVS AMPAQRRVVV ISGAGDRRDE DIRIQTEILG AAFDDVILYE
DACQRGREAG EVVALLRAGL QGASRTSYTE EIVGEFLAID RALARLQPGD LCLVLVDQVE
EALAHLAQRI SEG
//
