ID A0A1U7PXB4_9FLAO Unreviewed; 873 AA.
AC A0A1U7PXB4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SAMN05660493_01291 {ECO:0000313|EMBL:SIT96602.1};
OS Epilithonimonas bovis DSM 19482.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Epilithonimonas.
OX NCBI_TaxID=1121284 {ECO:0000313|EMBL:SIT96602.1, ECO:0000313|Proteomes:UP000187261};
RN [1] {ECO:0000313|Proteomes:UP000187261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19482 {ECO:0000313|Proteomes:UP000187261};
RA Varghese N.;
RL Submitted (OCT-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; FTPU01000011; SIT96602.1; -; Genomic_DNA.
DR RefSeq; WP_076782818.1; NZ_FTPU01000011.1.
DR AlphaFoldDB; A0A1U7PXB4; -.
DR STRING; 1121284.SAMN05660493_01291; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000187261; 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 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}.
FT DOMAIN 221..474
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 873 AA; 97044 MW; 6B4CD7240F9602FE CRC64;
MKIEKIQVLR GPNIWSITRK KLIQMRLDLE ETEHTPTNKI PGFRERIETL LPSMYTHRCS
EGTEGGFFKR VEMGTWMGHV IEHIALEIQT LAGMDVGFGR TRETKTPGTY NVVFNYIEES
AGVYAAEEAV KIAESLMNAT DYDINACIQT LKEIRERERL GPSTGSIVEE AASRKIPWIR
LGKNSLVQLG YGINQQRFQA TITGNTSCIA VDIACNKELT KKMLEDAAIP VPSGDLVLDE
EGLQRVIKKI GYPLVLKPLD GNHGKGASIN VKDYETALVG LEHAQKYSRK VIVEKYITGY
DFRVLVIDHR MVAAARRVPA HVMGDGELNL QQLIDKENED PRRGYGHENV LTEIEVDKDT
NELLAKLNYT LETVPQKGEI VYLKSTANLS TGGTSIDVTD MIHPENIQMA ERISRIIGLD
VCGIDIMAEN LTQPLKESGG AILEVNAAPG FRMHLAPSEG LPRNVAAPVV DMLYPPGKEF
RIPIIALTGT NGKTTTTRLL AHIVKNNGKR VGFTTSDGIY IHNTLLERGD TTGPLSAEFI
LKDPTVEFAV LETARGGILR SGLGFGTCDI GVLTNIKEDH LGISDIHNLK DLTRVKRVVL
DSVKKDGWCI LNADDDYSMR IMNDLHSKVA LFSLDENNPH IKKFAKEGKV TCVYEEGFVT
IKKGEWKIRI ERVKNIPITM DGKARFMIAN VLAASLAAYV YGFEIPNIAL ALTTFIPSAQ
LTPGRLNVFN FKNFKVMIDF AHNPAGYEAI EDYLKNVESN KKIGIISGVG DRRDSDIREC
GKIAARMFDH IIIRNEKHLR GRTEDEINGL IIDGIHSSGN NVSYEIIPKE IDALKHAMSL
AEEGTFITAL SDVINNAIEI VQEYQARELL DEQ
//
