ID A0A1H0Z6G9_9GAMM Unreviewed; 929 AA.
AC A0A1H0Z6G9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-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 ORFNames=SAMN05216569_0196 {ECO:0000313|EMBL:SDQ22968.1};
OS Pseudoxanthomonas sp. CF125.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1855303 {ECO:0000313|EMBL:SDQ22968.1, ECO:0000313|Proteomes:UP000199049};
RN [1] {ECO:0000313|EMBL:SDQ22968.1, ECO:0000313|Proteomes:UP000199049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF125 {ECO:0000313|EMBL:SDQ22968.1,
RC ECO:0000313|Proteomes:UP000199049};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNLD01000001; SDQ22968.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0Z6G9; -.
DR STRING; 1855303.SAMN05216569_0196; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000199049; 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; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
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; IPR013815; ATP_grasp_subdomain_1.
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; 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 Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000199049}.
FT DOMAIN 233..486
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 929 AA; 100499 MW; 9BE2605F0514B472 CRC64;
MRILERSVYV GPSQYAHFPV IRLELDLQAL EAWPTGKLGA AFVDGLIAAL PGLAEHGCSY
REPGGFIRRM REGEGTWLGH VLEHVAIELQ NVAGENVTFG KTRSVGDDRP GVYTVIYEYA
QKEEGIAAGE LALKLLSSLL PAELRPKDSV PGDWDWDTAR DDFIRYAQRR ALGPSTASLV
RAAEERGIPW LRLNQQSLIQ FGHGKYQQRI QATVTGKTPH ISVELASDKE ETNKILGSLG
LPVPRQELVN DASGALRAAR KLGGTVVTKP YNGNHGRGIT INISGEDEIR EGFAAAREHS
RSVIVETYIG GDDHRLLVVN GELIAATKRT PGHVIGDGKS DIAELVDQVN SDPRRGVGHE
KVLTRLELDA QADLMLERVG YNHFSVPKEG EVVYLRSTAN LSTGGTATDV TDIIHPDNRD
MAVRAVRAIG LDVGGVDFIS PNIAESYKSI GGGICEINAA PGFRMHVAPS EGTPRDAAGP
VIDMLFPPGT PTRVPIAAIT GTNGKTTTAR MLAHITKMAG YTPGLTTTDG VYIDGQRTVE
GDMTGPVSAR MVLSDPQIDM AILETARGGL LRSGMGVPEV DVGAVLNVAS DHLGLKGIDT
LEQLAEIKRI VVEVARDCAV LNADDPNVLK MSAYTDAKVI CYVTLNPSHT LVREHIRAGG
RACALEAGVN GHMITLYDKG SHIPLMWTHL IPATLEGRAL HNVQNAMVAA AMAFSLGIKL
DAIRQGLRTF DTTFFQAPGR MNVYSEHPFK VLMDYGHNAH AVGMMADLAQ RLDVTGRRIV
VLTGPGDRRD EDLRAIAEVV AGKFDHYVVR RDDALRGRDG DEVPRIIAKA LLSAGIAENA
MSIIPDEQEA IDAALRMGQP GDLILIFADA LTRSWKQIIK FQPQGEVAKA SPRVELPSLE
TSPEEAPFAS MEGVIREERG LVFEREDSD
//
