ID A0A1N7B3X6_9BACT Unreviewed; 880 AA.
AC A0A1N7B3X6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=SAMN05421545_3769 {ECO:0000313|EMBL:SIR45977.1};
OS Pontibacter lucknowensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=1077936 {ECO:0000313|EMBL:SIR45977.1, ECO:0000313|Proteomes:UP000185924};
RN [1] {ECO:0000313|Proteomes:UP000185924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DM9 {ECO:0000313|Proteomes:UP000185924};
RA Varghese N., Submissions S.;
RL Submitted (JAN-2017) 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; FTNM01000006; SIR45977.1; -; Genomic_DNA.
DR RefSeq; WP_076423216.1; NZ_FTNM01000006.1.
DR AlphaFoldDB; A0A1N7B3X6; -.
DR STRING; 1077936.SAMN05421545_3769; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000185924; 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:0008716; F:D-alanine-D-alanine ligase activity; IEA:InterPro.
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; IPR011810; Cya_phycin_syn.
DR InterPro; IPR044019; Cyanophycin_syn_N.
DR InterPro; IPR011095; Dala_Dala_lig_C.
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; PF07478; Dala_Dala_lig_C; 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.
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:UP000185924}.
FT DOMAIN 221..474
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 880 AA; 96998 MW; 4F96DE74F3404154 CRC64;
MKILELRIMR GPNYWSIKHP KIIVLKLDLE GLQDVLTNEV PQFPERLEKL FPGMYEHRSS
KGTPGGFFRL VREGTTFSKV VQHIALELQT LAGMNSGYGR RYAGPGPGVD YVVFSYQQER
AGEYAAHAAV RITELMAKGK KPSIVQDIAR LHQIREDEYF GPSTEAIVSE AVSRGIPYIN
NQRSGLIQLG YGIHQKHIQA AMTSRTSCFG VENAGNKNAT KLILEDAGIP VPRGHIVHDA
DELEEAVQEL GYPVVVKPLD GNQGKGATIN IHTWKEAQRA LTEAQRYSKK VMVEQFITGD
DYRLLVINGK FIAAAKRTPA MVTGNGISTI QQLVKEVNKD PRRGIGHEKA LTHIKIDKHT
RSLLKEKGLT LQSVLPEGEV LYLKSTANLS TGGTATDVTD LVHPYNVLMA ERIAGIIGLD
VCGIDVMTTD IAIPLPETKG AVIEVNAAPG LRMHISPTDG LPRNVAEPII NMLFPHSTPT
RIPIVAITGT NGKTTTTRLV AHMLKFKGYQ VGYTTTDGIY IQDNKIIKGD TTGSYSSEFV
LKDPTVNYAV LECARGGMLR SGLAFRQCDI GIVTNVSADH LGLGDINTVE EMAEVKAVIP
RTVCQNGYAV LNADDDLVFE MATGLSCKVA FFSLDENNPR ILQHISKGGL AAVLENGYIS
IFKNTYKIRV DRVADIPLTF GGRARFNIHN VLAATLTGYI NHFEIAEIRT ALRTFIPSAE
TTPGRMNLFK LPRYEVLIDY AHNIASMEAI ADFIDNVQAT YKIGIVAGIG DRQEEDTIEI
GRIAAETFDE IIIRQDKDLR GKSGQEINSL IKQGIMAVKP NMKLTEINQE TRALAHAMEY
APEGAFITLF SEDIPESIKL VESFRIIDHR RISSLEQDSF
//
