ID A0A0E3ZGL1_9BACT Unreviewed; 876 AA.
AC A0A0E3ZGL1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=PKOR_15255 {ECO:0000313|EMBL:AKD04199.1};
OS Pontibacter korlensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=400092 {ECO:0000313|EMBL:AKD04199.1, ECO:0000313|Proteomes:UP000033109};
RN [1] {ECO:0000313|EMBL:AKD04199.1, ECO:0000313|Proteomes:UP000033109}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X14-1T {ECO:0000313|EMBL:AKD04199.1,
RC ECO:0000313|Proteomes:UP000033109};
RX PubMed=26057562; DOI=10.1038/srep10929;
RA Dai J., Dai W., Qiu C., Yang Z., Zhang Y., Zhou M., Zhang L., Fang C.,
RA Gao Q., Yang Q., Li X., Wang Z., Wang Z., Jia Z., Chen X.;
RT "Unraveling adaptation of Pontibacter korlensis to radiation and
RT infertility in desert through complete genome and comparative
RT transcriptomic analysis.";
RL Sci. Rep. 5:10929-10929(2015).
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; CP009621; AKD04199.1; -; Genomic_DNA.
DR RefSeq; WP_046311854.1; NZ_CP009621.1.
DR AlphaFoldDB; A0A0E3ZGL1; -.
DR STRING; 400092.PKOR_15255; -.
DR KEGG; pko:PKOR_15255; -.
DR PATRIC; fig|400092.3.peg.3327; -.
DR HOGENOM; CLU_016806_0_0_10; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000033109; 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:UP000033109}.
FT DOMAIN 221..474
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 876 AA; 96246 MW; 445E4BD45A3699A1 CRC64;
MKILELKIMR GPNYWSIKHP KIIVLKLDLE DLQHTLTNEV PNLAQKLQKL FPNIYKHRSS
AGTEGGFIRL VNEGTTFSKV VQHIALELQT MAGMDSGYGR RYASSQPGVD FVAFSYQQER
AGEYAAEAAV RITDSLARGE RVSVIQDIAK LHQIREDEYF GPSTEAIVQE AVNRNIPYIQ
NRQSGHIQLG YGVNQKRIQA AMSSNTSCFA VENAGDKNIT KLILEEAGIP VPQGRIVYST
RELEDAIDEL DYPIVTKPLN GNQGKGASIN IQNWKDALKG FAEAQRYSEA VMVEQFIQGS
DYRMLVIDGK FIAAAKRTPA MVTGDGTSTI RQLVNQVNKD PRRGVGHEKA LTHIKIDKIS
RAILREKGLN LQSVLPAGEV LYLKRTANLS TGGTATDVTD IVDPYNILMA ERIAGIIGLD
ICGIDVMTSD IAIPLPETRG AVIEVNAAPG LRMHISPTEG LPRNVAEPII NMLFPFGCPA
RIPIVAITGT NGKTTTTRLI AHILSFKGYK VGYTTTDGIY IQGRKIIKGD TTGSYSSEFV
LKDPTVNYAV LECARGGMLR SGLAFTQCDV GVVMNVSEDH LGLGDINTVE DMARVKGIIP
KTVCSDGYAI LNADDELVYG MAAGLRCKVA FFSLDESNPR IIEHISKGGL AAVLEDGYIS
IFKNTYKIRV DRVADIPLTF GGKARFNIYN VLASTLAAYV SHMEINEIKT ALRTFIPSPD
TTPGRMNLFK LPKAEVLVDY AHNIAAMQAI SDFISNTGAH TKIGIIAGIG DRRDEDTREV
GRIAASVFDK IIIRQDKDLR GRSGEEINHL LKEGIFSVKP DMEPLEISQE TRALAYALEY
APEGSFIALF AEDIPEAVKL IENFRVIQHR KTTTEQ
//
