ID A0A363RSB2_9BURK Unreviewed; 860 AA.
AC A0A363RSB2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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:PWB20114.1};
GN ORFNames=DCO45_03385 {ECO:0000313|EMBL:PWB20114.1};
OS Comamonas sp. JNW.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=2170731 {ECO:0000313|EMBL:PWB20114.1, ECO:0000313|Proteomes:UP000251772};
RN [1] {ECO:0000313|EMBL:PWB20114.1, ECO:0000313|Proteomes:UP000251772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JNW {ECO:0000313|EMBL:PWB20114.1,
RC ECO:0000313|Proteomes:UP000251772};
RA Go L.Y., Mitchell J.A.;
RL Submitted (APR-2018) 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}.
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:PWB20114.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QETI01000002; PWB20114.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A363RSB2; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000251772; 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; 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 InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp.
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; PF01071; GARS_A; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SMART; SM01209; GARS_A; 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:UP000251772}.
FT DOMAIN 209..466
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 860 AA; 91962 MW; C33FBAAD6AC4413B CRC64;
MQLSRTRALR GPNLWTRSTA IETIVRCEDS EQRYSTIPGF EEKLRARFPN IAPLQPHGAD
QALSLAHVLE IAALSLQAQA GCPVTFSRTH VTTEPGTYQV VVEYTEEAVG KLAMEKAEAL
IQATLNDSPF DADAAIAALR ELDEDERIGP STGAIVDAAV ARGIPFRRLT SGSLVQLGWG
SKARRFQAAE IDSTSAVAES IAQDKDLTKR LLHAAGVPVP MGRPVADVEE AWRVALEVGL
PVVVKPQDGN QGKGVVVNIT TREGLEAAYK TASEFGDEIM VERFLPGHDF RLLVVGGQLV
AAARREPPQV LGDGQHTIRE LVNLVNQDPR RGTGHGTALT KIRLDDIAIA RIASEGMTPD
SVPGQGQRVV LRNNANLSTG GSATDVTDDV HPEIAARAIE AAQTIGLHIC GVDVVCETML
KPLEEQSGGI VEVNAAPGLR MHLAPSFGKP RHVGVPMVDE MFSAGNDGRI PLVAVTGTNG
KTTTTRVIAH LFTSHGWRTA MTNTDGVYVN GRQIDSGDCS GPRSARNALA HPETDAAVLE
CARGGILREG LGFDRCQVAV VTNVGEGDHL GLNFITTKED VGVLKRVIVQ NVAPTGYAVL
NAADPLVAAM AHVCPGKVIF FAADRHHPVM ATHRAQGSRV VYVDGDSIVA AEGSWRESIP
LREIPITRNG AITFQVENVM ASIGAAWAAG LPWQTIRRGL AGFVNDSDNA PGRFNVMDYR
GATIIADYGH NPDAIRALIQ AVEAMPANKR SVVISGAGDR RDEDIRVQTE MLGEAFDDVI
LYQDAAQRGR ADGEVIALLR QGLQGASRTS YVTDIHGEFI AIDHALARLQ PGDLCLVLVD
QVEEALEHLQ RHVAQAAAQA
//
