ID A0A0S9Q4L8_9ACTN Unreviewed; 922 AA.
AC A0A0S9Q4L8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=ASF47_13155 {ECO:0000313|EMBL:KQP64829.1};
OS Nocardioides sp. Leaf285.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736322 {ECO:0000313|EMBL:KQP64829.1, ECO:0000313|Proteomes:UP000051495};
RN [1] {ECO:0000313|EMBL:KQP64829.1, ECO:0000313|Proteomes:UP000051495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf285 {ECO:0000313|EMBL:KQP64829.1,
RC ECO:0000313|Proteomes:UP000051495};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP64829.1, ECO:0000313|Proteomes:UP000051495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf285 {ECO:0000313|EMBL:KQP64829.1,
RC ECO:0000313|Proteomes:UP000051495};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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}.
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:KQP64829.1}.
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; LMNH01000003; KQP64829.1; -; Genomic_DNA.
DR RefSeq; WP_056864371.1; NZ_LMNH01000003.1.
DR AlphaFoldDB; A0A0S9Q4L8; -.
DR Proteomes; UP000051495; 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 CDD; cd01983; SIMIBI; 1.
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:UP000051495}.
FT DOMAIN 229..484
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 899..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 922 AA; 100126 MW; 2102FF8F8E984260 CRC64;
MTERPTPDLS ILETRVYRGA NVWSYDRAIH LVIDLGVLEK FPTNTVPGFT ETLLQMLPGL
REHSCSRGRR GGFVERLHEG TWLGHVAEHC ALALQQVVGH DVRRGKTRMV KGRPGVYNVV
YGYIDEQVGL AAGRLAVRLV NHLVEADPEF DWDTSLEEFI RRAQRTAFGP STQAILDEAV
SRDIPWIRLN QYSLVQLGQG VHAKRIRATM TSATSAIAVD IASDKDLTTT LLGAAGLPVP
KQESVRTVEQ CVRAAQRIGY PVVVKPLDGN HGRGVCLDLQ DEAEVREAYE VARAESRRGV
LIVESLITGK DYRCLIIDGK VAAIAERVPA SVTGDGTSSV EQLVDDANAD PRRGVGHEKV
LTRIKVDAAA VELVREQGFE MSDVPPAGTM VKLALTGNMS TGGISIDRTF EAHPENVEIA
EEAARMVGLD IAGIDFICPD ITEPVRETGG AICEVNAAPG FRMHTHPTIG EPQFIAKPVV
DMLFPPGAQS RIPIVAVTGT NGKTTTSRMI SHIFKGMGRK VGMTSTDGVV IDERLLIRSD
ASGPRSARMV LQNPRVDFAV FEVARGGILR EGLGYERNDV AVVLNVQPDH LGLRGIDTVE
QLADVKAVLV EAVPRDGHAV LNADDPLVRD MRRRCSGQVV WISMEEPGSE VRDMIDAHCR
RGGKALVLNS SERGEMIVVK HGPREMQLAW THLLPATFNG RARMNVQNVL AAAAAAFAAG
APLHDIRQGL RTFSTNYYLS PGRLNEVEVN GVNVIVDYCH NAPGMRALGD FVDRVGDSMA
GSHELARPSR IGVIATAGDR RDQDMRELGE IAAQHFDVVI VREDAQLRGR ERGDVSALVT
EGVRSAMAEG SRCKQVEVVL DEIEAVRHAM SRANRGDLVV ICVDKHGEVM TELENWSPHA
QAGSGVSADA PAADPDYVPS EA
//
