ID A0A1Y0M8P4_9FLAO Unreviewed; 886 AA.
AC A0A1Y0M8P4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=BTO04_08145 {ECO:0000313|EMBL:ARV06664.1};
OS Polaribacter sp. SA4-10.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=754397 {ECO:0000313|EMBL:ARV06664.1, ECO:0000313|Proteomes:UP000195822};
RN [1] {ECO:0000313|EMBL:ARV06664.1, ECO:0000313|Proteomes:UP000195822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA4-10 {ECO:0000313|EMBL:ARV06664.1,
RC ECO:0000313|Proteomes:UP000195822};
RA Kumagai Y., Yoshizawa S., Kogure K., Iwasaki W.;
RT "Trade-off between light-utilization and light-protection in marine
RT flavobacteria.";
RL Submitted (DEC-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; CP019331; ARV06664.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0M8P4; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000195822; Chromosome.
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; 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 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 Pfam; PF08443; RimK; 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:UP000195822}.
FT DOMAIN 221..476
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 886 AA; 97399 MW; 4C0303212B26DEC9 CRC64;
MRIREINAMR GPNYWSVRRH KLIVMVLDLE EMEERPSNKV EGFSERLKAM FPTMYSHRCS
EGCAGGFFMR VDEGTWMGHI IEHIALEIQT LADMDTGFGR TRGYGEEGVY SVVFSYIEEN
VGRYAAKAAV KICEALIEGE PYDLTDDIQE MRELRESSRL GPSTGSIVAE AEARGIPWLR
LNKYSLCQLG YGANQKRIQA TVTSETSSIG VELACDKEDT KYLLEQAEVA VPKGDIIKRE
SSLKEACRYV GYPLVIKPID GNHGRGITVD IQNYEDALEG FKHAKNSSKS GAIIVEKFIT
GEDYRLLVIN NVLVAAAKRT PAHVIGDGNS SVETLIDEVN KDSRRGYGHE NVLTKITINE
LTKTIIKDAG YTLESVLKKE EMLILKDTAN LSTGGTAEDV TDIVHPANIA MAERISKIID
LDICGIDIMS TDISKPLADT GGAVLEVNAG PGFRMHLAPT EGLPRNVAAP VIDKLFPPGS
TSRIPIVAVS GTNGKTTTTR LIAHMAKMKG YKVGYTTSDG VYIQNRLLMT GDCTGPASAE
FVLRDPTVNF AVLESARGGL LRAGLGFKNC DIGIVTNVAA DHLGLKGIHT IEQLAKVKAV
IPETVLPDGT AILNADDELV YAMRKNLDCN VALFSLDENN PHIKALQKIG GISAIYENGY
ITICRGTWKI RVIKAVNVPL TYGGKATFMI QNVLPAVITA YLRGFSIEDM KMSLETFIPS
ATQTPGRLNL FKFKNFQILL DYAHNAAGMR ALKQFTDNLE ATVKVGIIAG IGDRRVEDNN
EMGGIASEMF DEIIIRQDKH LRGKTEEELI KMLKDGITSK DKDKKITIIP SEREAILYAV
KNAKKGALIV LCSDVVPDAL NLVKELKEKE ANELYEFKTE DIPNQH
//
