ID A0A1G9Q5A7_9SPHI Unreviewed; 871 AA.
AC A0A1G9Q5A7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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 ORFNames=SAMN05421813_105107 {ECO:0000313|EMBL:SDM05535.1};
OS Daejeonella rubra.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Daejeonella.
OX NCBI_TaxID=990371 {ECO:0000313|EMBL:SDM05535.1, ECO:0000313|Proteomes:UP000199226};
RN [1] {ECO:0000313|Proteomes:UP000199226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24536 {ECO:0000313|Proteomes:UP000199226};
RA Varghese N., Submissions S.;
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; FNHH01000005; SDM05535.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9Q5A7; -.
DR STRING; 990371.SAMN05421813_105107; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000199226; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000199226}.
FT DOMAIN 221..474
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 871 AA; 96567 MW; B76320941381AEA2 CRC64;
MKILGIQVLK GPNIWSTRRK KLIQMRLDLE DLEQRPTNKI EGFRERIEKL MPSLFTHRCS
PGYEGGFFER VEEGTWMGHV IEHIALELQS LAGMETGFGR TRETKTPGTY NVVFNYIEET
VGVYAAEASV RIAEAIISGD EYDIENDIMT MKKMRERERF GPSTASIVDE AVARKIPFIR
LNRSSLVQLG YGVNQVRFRA TMTDKTSSIA VDIAGNKDET KRILQEQAIP VAKGMTISSD
EDLEIALTQI GFPLVFKPLN GNHGKGATIN VKTREEAIEA FAYAQKYSHR VILERFITGH
DFRILVIDNR MVAAAQRVPA NVVGDGSNSI QKLIDIENSD PRRGYGHENV LTEITVDRDT
LDLLDKKGYT LETVPPKSEI VYLKSTANLS TGGTSIDVTD MVHPQNVFMC ERIARVIGLD
ICGIDIMAKN LTELLTENGG VVLEVNAAPG FRMHLAPSEG LPRNVAAPVI DMLYPPGKSA
RIPIIAVTGT NGKTTTTRLI AHIVKNNGFR VGFTTSDGVY IQNSMLLKGD TTGPISAEFV
LKDPTVEFAV LETARGGILR SGLGFGLCDI AVITNIQEDH LGISDIHTLE DLARVKQVVV
NSVKNDGWAI LNADNKHCVK IGKDVHCNVA YFTMDEKNPV VKEHCRKGGI AAVYENGFVT
IKKGDWKIRI EKVTHIPITF NGTVGFMTQN VLAASLATFV WGFKIEDIRL SLETFIPSAA
QTPGRMNIFE LKECKIMVDF AHNPDGLRGI KDFLSTLDIK RSTGIISGTG DRRDEDLREI
GRISAEMFDN VIICQEKYLR GRDRDEIVKL IIEGLKEVKP EIDIQIINKG KDAFNHAVKH
IIPGSFVTII GDSVSNAVEL VQDYQDKEIG I
//
