ID A0A0G3ERQ1_9BURK Unreviewed; 860 AA.
AC A0A0G3ERQ1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=ABW99_11250 {ECO:0000313|EMBL:AKJ68704.1};
OS Pandoraea thiooxydans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Pandoraea.
OX NCBI_TaxID=445709 {ECO:0000313|EMBL:AKJ68704.1, ECO:0000313|Proteomes:UP000036700};
RN [1] {ECO:0000313|Proteomes:UP000036700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25325 {ECO:0000313|Proteomes:UP000036700};
RA Lim Y.L., Ee R., Yong D., How K.Y., Yin W.F., Chan K.G.;
RL Submitted (JUN-2015) 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; CP011568; AKJ68704.1; -; Genomic_DNA.
DR RefSeq; WP_047214567.1; NZ_CP014839.1.
DR AlphaFoldDB; A0A0G3ERQ1; -.
DR STRING; 445709.ABW99_11250; -.
DR KEGG; ptx:ABW99_11250; -.
DR PATRIC; fig|445709.3.peg.2392; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000036700; 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:UP000036700}.
FT DOMAIN 209..462
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 860 AA; 91755 MW; 0A79611B79648FD7 CRC64;
MEVSRIRALR GPNLWSRRTA IEAIVKCTEA ECSIDNLPGF EARLRSRFPE IGMLQPEGIQ
QPLSLAHALE AAALGLQAQA GCPVTFSRTA ATVEPHVYQV VVEYTEEAVG RFAFELAEVL
CRAAKRDTSF DLADALARLR ELDEDVRLGP STGAIVSAAV ARGIPYHRLT EGSMVQFGWG
SRARRIQAAE SSATSAIAES IAQDKELTKS LLAVAGVPVP QGRTVVDAED AWAAACEIGG
QVVVKPRDGN QGKGVAVNIE SREQIMTAYE AAAQISSEVI VERHIAGHDF RLLVVGDKLV
AAARRDPPQV IGDGVQTIRE LVEQINCDPL RGEGHATSLT KIRLDEIALA TLDKQAYTAD
SVPPKGKRVV LRNNANLSTG GTATDVTDDV HPEVAERAIA AAQMVGLDIC GVDMVCETVH
KPLEEQGGGI VEVNAAPGLR MHLSPSYGKS RAVGEAIISA MFDGDDDGRV PVVAVAGTNG
KTTTVRLTAH LLAASGRRVG MTNSDGVYIQ KQRIDTGDCS GPKSARNVLM HPDVDAAVLE
TARGGILREG LGFDRCDVAI VTNIGMGDHL GLNFISTVED LAVVKRVIVQ NVAPHGTAVL
NAADPMVANM ADTCPGSVIY FARERNHPVM ATHRAQGKRV VYTENGHIVA AEGHLEYRVA
LTTVPLTANG LITFQVENAM AATAAAWALG LDWDTIRAGL ATFVNDAGTA PGRFNMFDYH
GATLIADYGH NPDAILALVD AIDALPAKRR VTVISGAGDR RDVDIRRQTE ILGDAFDEVI
LYEDQCQRGR ADGEVLALLR EGLKNAKRAA VTEEVRGEFL AIDMALERLA PGDLCLILVD
QVEEALTHIA QRIAEADNAA
//
