ID A0A221KJ29_VITFI Unreviewed; 857 AA.
AC A0A221KJ29;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=VITFI_CDS3033 {ECO:0000313|EMBL:ASM78810.1};
OS Vitreoscilla filiformis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Vitreoscilla.
OX NCBI_TaxID=63 {ECO:0000313|EMBL:ASM78810.1, ECO:0000313|Proteomes:UP000199729};
RN [1] {ECO:0000313|EMBL:ASM78810.1, ECO:0000313|Proteomes:UP000199729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15551 {ECO:0000313|EMBL:ASM78810.1,
RC ECO:0000313|Proteomes:UP000199729};
RA Contreras S., Sagory-Zalkind P., Blanquart H., Iltis A., Morand S.C.;
RT "Complete Genome Sequence of the cosmetic ferment Vitreoscilla filiformis
RT (ATCC15551).";
RL Submitted (JUL-2017) 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; CP022423; ASM78810.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A221KJ29; -.
DR KEGG; vff:VITFI_CDS3033; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000199729; 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; 3.30.1490.20; 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; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
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; PF02786; CPSase_L_D2; 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.
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:UP000199729}.
FT DOMAIN 207..459
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 857 AA; 91190 MW; 1A4DB0AE5604466A CRC64;
MDISRIRALR GPNLWSRHTA VEAIVACEPH ECALTDLPGF EARLRALFPG LGALRQAPEQ
SSLAHVLETA TLALQAQAGC PVSFSRTTQT VEAGTYQVVV EYSEEPVGRK ALAAAEALIQ
AALSEGSFDV DATLAELREL DEDVRLGPST GSIVQAAVAR GIPFRRLTSG SLVQLGWGSK
ARRIWAAEVD STSAVSESIA QDKDLTKTLL RAAGVPVPLG RPVDSVDEAW EVAQEIGLPV
VLKPQDGNQG KGVTVNIVSR EHLEVAYKAA EDIGQVMVEK YLPGSDFRLL VVGNKLVAAA
RRDPPQVIGD GIHTVRQLVE QVNADPRRGD GHATSLTKIR FDDIAVARLA LQDLQPDSVP
EKGRRVILRN NANLSTGGTA TDVTDDVHPE VAARAVAAAQ MIGLDICGVD VVCENVIRPL
EEQSGGIVEV NAAPGLRMHL SPSFGKGRAV GEAVINHLYA PGEDGRIPVI AVTGTNGKTT
TTRLVTHLLA ASGLRVGMTN TDGVHVNGRQ IDSGDCSGPK SARNVLMNPD VDAAVFETAR
GGILREGLGY DRCQVAVVTN IGAGDHLGLN YITTVEDLAV LKRVIVQNVA PNGYAVLNAT
DAHCVPMAKV CPGDVIYFAP DRHHPVLATH RAQGKRCIYV ENGHIVACEG NWRENLPLAE
VPLTRGGLIT FQIENAMAAV GAAWGVGLSW DAIRAGLASF VSDSDNAPGR FNLMDYHGAT
LIADYGHNPD AMRALVSAVN ALPGQRRSVV ISGAGDRRDE DIREQTQILG AAFDDVILYQ
DACQRGREDG EVLGLLRQGL EGAPRTTHTE EVRGEFAAID RALSRLRPGD LCLVLVDQVE
EALAHLAQRM GEPPLGA
//
