ID A0A1I7KR78_9BACL Unreviewed; 883 AA.
AC A0A1I7KR78;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN05421543_11838 {ECO:0000313|EMBL:SFU99908.1};
OS Alicyclobacillus macrosporangiidus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=392015 {ECO:0000313|EMBL:SFU99908.1, ECO:0000313|Proteomes:UP000183508};
RN [1] {ECO:0000313|Proteomes:UP000183508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17980 {ECO:0000313|Proteomes:UP000183508};
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 -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FPBV01000018; SFU99908.1; -; Genomic_DNA.
DR RefSeq; WP_074954746.1; NZ_FPBV01000018.1.
DR AlphaFoldDB; A0A1I7KR78; -.
DR STRING; 392015.SAMN05421543_11838; -.
DR eggNOG; COG0189; Bacteria.
DR eggNOG; COG0769; Bacteria.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000183508; 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:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000183508}.
FT DOMAIN 219..472
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 883 AA; 95233 MW; 11FA387D4F809144 CRC64;
MNIVSVRHLD GPNIYIYKPV MVARVDLEGL TERESYEFPG FPDRLLRTLP GLREHHCAKG
APGGFVERLY GGTYFGHIVE HVAIEFACLA GVDVHFGRTV YAGRPGLYDI VMECKAYPCQ
RYLLQAAIGL VEDLLEGVSP SLDAVLAEAE RILAGTELGP STRAIAEAAS RRNIPVRRLN
EGSLIQLGYG KHRKLVEATV TERTSAVSVD IACDKELTKR LLAEAGIPVP DGEVADDAEG
AVAALRRMGP PVVVKPFNGN QGRGVSLDLH SEQEVREAYD IASAISPRVL VERYVQGRNI
RFLVVDGRFA AASERIPARV FGDGVHTVRE LIERANADPL RGMGHEKPLT RIQVDAVVTS
TLRRQRLSLS SVPAAGQEVL LRASANLSTG GEAIDVTGDV HESYVRLAER IARIIGLDVC
GIDMVVARPE APWDRNGCTV IEVNAAPGIR MHEHPSYGLP RAVGERIVES LFPNGADGRI
PIVSITGTNG KTTTTRLIAH VLAATGRTVG MTTTSGVWIG GERVLEGDTT GPNSARVVLS
DPAVEVAVLE TARGGIVRGG LAYDRANVAV ITNIRVDHLG QDGVETLEDL VHIKSLVGEC
VWEDGTVVLN ADDEHLVELA PRLPAQVAYF SMSDQNPVLK RHLACGGVGY YVSRGWIVEG
RGNLTWEVAP VRDIPLTMQG LARFHTENCL AAVAALRALG CTRQQVASGL TTFLPSEHNP
GRCMLYRLPG GAYAVLDYGH NPDGFQRMGE WLKQVPHRRL IGVVGVPGDR MDSVIRQSGR
QAAEIFDAFV VKEDADKRGR RDGEVAALLA EEIQALAPGK PCTVIAREPE ALRFALSQAV
AGDVVVMFFE QLAPAQEVVR AFDGVPVAGF DVTPAQPFAA IPL
//
