ID A0A2S1R284_9FLAO Unreviewed; 875 AA.
AC A0A2S1R284;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, 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 Name=cphA {ECO:0000313|EMBL:AWH86689.1};
GN ORFNames=HYN59_16950 {ECO:0000313|EMBL:AWH86689.1};
OS Flavobacterium album.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2175091 {ECO:0000313|EMBL:AWH86689.1, ECO:0000313|Proteomes:UP000244929};
RN [1] {ECO:0000313|EMBL:AWH86689.1, ECO:0000313|Proteomes:UP000244929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HYN0059 {ECO:0000313|EMBL:AWH86689.1,
RC ECO:0000313|Proteomes:UP000244929};
RA Yi H., Baek C.;
RT "Genome sequencing of Flavobacterium sp. HYN0059.";
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}.
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DR EMBL; CP029186; AWH86689.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S1R284; -.
DR KEGG; falb:HYN59_16950; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000244929; 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:0004326; F:tetrahydrofolylpolyglutamate synthase activity; 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; IPR018109; Folylpolyglutamate_synth_CS.
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.
DR PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 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:UP000244929}.
FT DOMAIN 221..474
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 875 AA; 96654 MW; 13521816FCD81DCA CRC64;
MKILKIQALR GPNIWSVYRK KLIQMRLDLE ETEQTPTNLI PGFRERIEAL IPSLVTHRCS
EGVRGGFFMR IERGTWMGHV IEHIALEIQT LAGMDTGFGR TRETKTPGIY NVVFSYLEEN
VGIYAAEASV RIAEALIAGT EYDIDADIQE MRKIRERDRL GPSTGSIVEE AVARDIPWIR
LGSNSLVQLG YGINQMRFQA TITNKTSHIA VDIACNKEAT KRMLEAASIP VAGGGICTDE
AELEDIIKKI GYPIVLKPLD GNHGKGASIN VTNLEDAKAG LVFAQKYGRR VIVEKFITGF
DFRVLVIDNK VVAAAQRVPA HVKGNGKNTI QELIDIENTD PRRGYGHENV LTEISVDRDT
TDLLEKMGYT LETVPSKDEI VYLKSTANLS TGGTSVDVTD LMHPENIFLS ERIARVIGLD
VCGIDIMAEN LTQPLKENGG VILEVNAAPG FRMHLAPSEG LPRNVASPVI DMLYPPGKPS
RIPIFAVTGT NGKTTTTRLL AHIVKNNGFK VGFTTSDGIY VQNHMLEKGD TTGPFSAEYI
LKDPTVEFAV LETARGGILR SGLGYSRCDI GIITNIQEDH LGLNDIHTLD DLSRVKRVVV
RSVKKDGWAI LNGDDAECIK IGKDLDCNVA YFSMDEDSPF IKELAKEGRT TAVYENGFIT
IKKGEWKIRI EKASHVPLTL GGKAKFMIAN VLAASLASYL WGFKTDDISL SLQTFIPGAA
QTPGRMNIFN FRKFNVLIDF AHNPAGYRAV EDFLQNVEAT HKIGIIAGVG DRRDEDIREC
AEIAARMFDH IIIRQEKHLR GRTDENINGL IMEGIQRSGR NTTHEIIAKE TDAIKHAIDN
AKDGSYITAL SDVVANAIEI VQGYLDRENE EILSE
//
