ID A0A3D8LH85_9BACT Unreviewed; 878 AA.
AC A0A3D8LH85;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
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:RDV16800.1};
GN ORFNames=DXT99_03200 {ECO:0000313|EMBL:RDV16800.1};
OS Pontibacter diazotrophicus.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=1400979 {ECO:0000313|EMBL:RDV16800.1, ECO:0000313|Proteomes:UP000256708};
RN [1] {ECO:0000313|Proteomes:UP000256708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H4X {ECO:0000313|Proteomes:UP000256708};
RA Liu Z.-W., Du Z.-J.;
RL Submitted (AUG-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:RDV16800.1}.
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DR EMBL; QRGR01000003; RDV16800.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8LH85; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000256708; 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: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 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.
DR PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ligase {ECO:0000313|EMBL:RDV16800.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000256708}.
FT DOMAIN 221..474
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 878 AA; 96460 MW; 07F31E5E12931E16 CRC64;
MKIAELRIMR GPNYWSIKHP KIIVLKLDLE DLQDTLTNEV QHLAQKLEKL FPGMYKHRSS
VGTEGGFFRL VHEGTTFSKV VQHIALELQT MAGMECGYGR RYAANEPGMD WVVFSYQQER
AGEYAAEAAV RITEALASGE RVSVIQDVAK LHQIREDEYF GPSTEAIILE AVSRNIPYIQ
NRKSDHIHLG YGVHQQRIQA AMSNKTSFFA VECAGDKNTT KLILDDAGIP VPQGHIVYDA
AELEAAVEEL GYPIVTKPLD GNQGKGASIN LQTWKDALKG LAEAKRFSNA VMVEQFIQGD
DYRMLVIDGK FIAAARRTPA MVTGDGQSTI RQLVNAVNKD PRRGVGHEKA LTHIKIDKIT
RGILREKGLT LQSVLSAGET LYLKNTANLS TGGTATDVTD IVHPYNVLMA ERIAGIIGLD
ICGIDVMTSD IAIPLPETRG AVIEVNAAPG LRMHISPTEG LPRNVADPII NMLFPYGCPS
RIPIVAVTGT NGKTTTTRLI AHMLKFKGKK VGFTTTDGIY IQDRKIVKGD TTGSFSSEFV
LKDPTVDYAV LECARGGLLR SGLAFTQCDI GIVTNVSADH LGLKDINTVE DMAKVKAVIP
KTVCPDGYAI LNADDDLVYN MAIGLRCKVA YFSMDEENFR IKEHISKGGL AAVFEDGYIS
IFKNTYKIRV DRVADVPLTF GGKARFNIQN VLAATLTGYI AHLEVGEIKT ALRTFIPSAE
TTPGRMNLFH LPKCNVLIDY AHNAAGMEAI SDFISQMEGY PKIGIIAGIG DRRDEDTRDV
GKIAASVFDE IIIRQDSDLR GRNGKEINNL LKEGIFSVKP EMEPKEISQE ARALAYALEY
APEGAFITLL AENISEAVKM VESFRIIQHR KQATDQLT
//
