ID A0A2S0PCM7_9NEIS Unreviewed; 876 AA.
AC A0A2S0PCM7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
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 {ECO:0000313|EMBL:AVY95083.1};
GN ORFNames=DAI18_14300 {ECO:0000313|EMBL:AVY95083.1};
OS Microvirgula aerodenitrificans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Aquaspirillaceae; Microvirgula.
OX NCBI_TaxID=57480 {ECO:0000313|EMBL:AVY95083.1, ECO:0000313|Proteomes:UP000244173};
RN [1] {ECO:0000313|EMBL:AVY95083.1, ECO:0000313|Proteomes:UP000244173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BE2.4 {ECO:0000313|EMBL:AVY95083.1,
RC ECO:0000313|Proteomes:UP000244173};
RA Anderson E., Jang J., Ishii S.;
RT "Denitrifier Microvirgula.";
RL Submitted (APR-2018) 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; CP028519; AVY95083.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0PCM7; -.
DR STRING; 1122240.GCA_000620105_01429; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000244173; 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:0009059; P:macromolecule biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
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; IPR013815; ATP_grasp_subdomain_1.
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; PF13549; ATP-grasp_5; 1.
DR Pfam; PF18921; Cyanophycin_syn; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 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 Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000244173}.
FT DOMAIN 224..473
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 876 AA; 95086 MW; 37991FBC969DFC41 CRC64;
MKKKDIEILR VISLRGPNMW TYRPVLEAWV DIGELEECPS NTLPGFYERL SSWLPSLIEH
RCSYGERGGF LRRVEEGTWP GHILEHVTLE LQNLAGMPGG FGKARETPIR GVYKVVVRAW
HEDVTRAALY AARDLVMAAI EDRPFDVAAV VDTLRDLVDD HCLGPSTACI VDAADDRDIP
YFRLNTGNLV QLGYGARQRR IWTAETDRTS AIAESISRDK DLTKTLLEAC GVPVPEGRYV
RSPEDAWEAA EEIGVPVVVK PYDGNHGRGV FTNLNTREEV EAAYKVAIDE GSGVIVERFV
EGLEHRLLVV GGKLVAAARG EEAWVVGNGR ETVRELIDSQ LNSDPRRGRT EDHPLNTVRL
DTAARLDLKR QGFEPDSVVP AGVDVLIQRN GNVAFDVTDI VHPEVAAAVS LAARTVGLDI
AGVDLVTRDI TRPLEEQRGA IVEVNAGPGL LMHLRPADGT PRPVGRAIAA HLFPEGEDGR
IPIVGITGSN GKTVVARLVA RLLRLSGAHV GLACSDGLFL DRRQVETRDS ANWDAARRIL
MNRAVDAAVF ENDSGALLND GLAYDRCQVG IITNIDNPDH LGDNHIDTAD RMFNVLRTQI
DVVLPTGAAI LNARDTDVAE MAALCDGEVI YFALDADLPV VQEHLAAGKR AVVVRDEQVV
LATGSDEIVL AQVDDFPLTR GGRVAFQTEN VLAAIAAAWS MGLSTDLIRA GIVTFEPDRH
DATGRFSVFE SQGSTVIVDD AHNPAALQAL VDALGRFPCS HRTVVYGGGV DRRDEDLVRQ
GEILGAAFDR IVLTDDATVS SQRPAGAARA LLRQGLAQAI RASDIREESD ATRAVDDALA
ALSAGECLII QCDEGNPRPV LNAVRQWAGQ QTPNNR
//
