ID W7WBI3_9BURK Unreviewed; 855 AA.
AC W7WBI3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
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 Name=cphA_2 {ECO:0000313|EMBL:EWS60001.1};
GN ORFNames=Y694_02195 {ECO:0000313|EMBL:EWS60001.1};
OS Methylibium sp. T29-B.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=1437443 {ECO:0000313|EMBL:EWS60001.1, ECO:0000313|Proteomes:UP000019360};
RN [1] {ECO:0000313|EMBL:EWS60001.1, ECO:0000313|Proteomes:UP000019360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T29-B {ECO:0000313|EMBL:EWS60001.1,
RC ECO:0000313|Proteomes:UP000019360};
RA Gyula P., Szabo Z., Robotka H., Bihari Z.;
RT "Genome sequencing of the loss-of-function mutant Methylibium sp. T29-B.";
RL Submitted (DEC-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EWS60001.1}.
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DR EMBL; AZSN01000049; EWS60001.1; -; Genomic_DNA.
DR RefSeq; WP_036232040.1; NZ_AZSN01000049.1.
DR AlphaFoldDB; W7WBI3; -.
DR PATRIC; fig|1437443.4.peg.2228; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000019360; 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: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; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ligase {ECO:0000313|EMBL:EWS60001.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 209..461
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 855 AA; 90654 MW; FEC73DE6566FE32D CRC64;
MEVSRIRALR GPNLWSRHTA IEAIVSCTAP ECEIADPVGL EARLRALFPT IGALRTAVPG
VPVSLAHLLE AAALALQAQA GCPVTFSRTS ATVDPGVFQV VVEYSEEEVG RLAFDLAREL
IDAALHARGF DVDAAITRLR ETDEDVRLGP STGAIVDAAL ARNIPYRRLT QGSMVQFGWG
SRQRRIQAAE VDSTSAVSEA IAQDKDLTKT LLRAAGVPVP IGRLVASADE AWAVALEIGL
PVVVKPQDGN QGKGVTVNIV DRAHLDVAFK AAAEIGDVMV EKFLPGSDFR LLVVGDRLVA
AARREPPHVI GDGVHTVREL VDLVNADPRR GTGHATSLTK IRFDEIAVAR LQVQGLAPDS
VPEKGRRVIL RNNANLSTGG TAADVTDDVH PEVAARAVAA AQMIGLHICG VDVVCETVGR
PLEEQSGGVV EVNAAPGLRM HLSPSFGKGR NVGEAMIQHL FGHGDDGRIP VVAVTGTNGK
TTTARLIAHL FATSGLRVGM TNTDGVYVEG RQIDSGDCSG PKSARNVLMH PDVDAAVFET
ARGGVLREGL GFDRCQVAVV TNIGSGDHLG LNYITTVEDL AVLKRVIVQN VAQSGYAVLN
ATDVNVAAMA GTCPGDVIFF AADRHHPVMA THRAQGKRTV YVEGDALVAA QGAWREKLLL
RDIPLTRGGT IGFQVENAMA AVAAAWGAGL DWDTVRRGLA SFVNDADNAP GRFNVMDFKG
ATVIADYGHN PDAMRALVAA VDAMPATRRA VVISGAGDRR DDDIREQTQI LGAAFDDVLL
YQDAAQRGRA DGEVIALLRE GLRGATRTRH VEEIHGEFIA IDTALDRLKP GELCLVLVDQ
VEEAMAHLAR RVAAG
//
