ID A0A1M5PVT3_9FIRM Unreviewed; 885 AA.
AC A0A1M5PVT3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-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=SAMN02746098_00043 {ECO:0000313|EMBL:SHH05756.1};
OS Desulfosporosinus lacus DSM 15449.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=1121420 {ECO:0000313|EMBL:SHH05756.1, ECO:0000313|Proteomes:UP000183954};
RN [1] {ECO:0000313|EMBL:SHH05756.1, ECO:0000313|Proteomes:UP000183954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15449 {ECO:0000313|EMBL:SHH05756.1,
RC ECO:0000313|Proteomes:UP000183954};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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 -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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; FQXJ01000003; SHH05756.1; -; Genomic_DNA.
DR RefSeq; WP_073026905.1; NZ_FQXJ01000003.1.
DR AlphaFoldDB; A0A1M5PVT3; -.
DR STRING; 1121420.SAMN02746098_00043; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000183954; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:0004363; F:glutathione synthase activity; IEA:InterPro.
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; IPR004218; GSHS_ATP-bd.
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; PF02955; GSH-S_ATP; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 220..473
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 885 AA; 97380 MW; 7958B444045BCE1F CRC64;
MEIREIQTIE GANVYSHRPI IRAIVDLQEW TERFTNELED FGKRLVEHLP TLDEHYCSRG
KRGGFLERLQ EGTLIGHVIE HVTIELLTQA GQSIKYGKTM VILDQPGWYE IIFNYEAKAG
AIEGFKQGFL LVQTLLNQNT FDVSRAVEQI KAVMAKCELG VSTQVIVDAC KERGIPVHRL
NEGSLLQLGY GRNQRRIQAT ITDATSSIGV DIACDKEMTK KILSEGGVPV PCGHIVRTEE
EAVEAFLDMG TTVVIKPLHG NQGKGVTLQL TNAAEVRAAF KVAQTYGEWV IIEEYIEGQH
YRLVVVGERL IAAAKRVPAH VTGDGKSTIE ELVVQTNADP LRGDDHEKVL TKIKIDSVVL
LNLTLKNLTL SSVPEKGEVV YLRDSANLST GGIAEDVTDL VHPDNVDLAV YASKLIGLDV
AGIDLVIEDI EASYRERSGH IIEVNAAPGI RMHHFPSKGK ARNVGKAIVE QILPAGNGRI
PIVAISGTNG KTTTTRMIGK LLADQQLLVG MASTDGIYIN KKMWVKGDTT GPESAKAVLR
HPQVQVAVLE TARGGILRSG LGYDYADVAV ITNVSNDHLG QYGIETLDDI AHVKSLIAEV
VMPHSYVVLN ADDPYVVQMA KRTQGRVIFF STEKDNIHIR KHLGKGGTAV FVRRGTILLC
QGSEVFRICS VKQIPVTWDG KAKHNIQNTL AAIASGWALG IGTATIRDSL QEFSSDAEHN
RGRLNLYELD GVQVFIDYGH NAAGIQEIAK TLKQFKKKSL VGCITVPGDR PDETVREVGR
IAAKGFQRLI IREDSDLRGR KPGEIAQLLY DEAILCGMDP KKIKVVLPEI EAFSQGLDSC
VPGDTFVMFY EHLEPIEEEI RKRMELQKAL SYIPSQNDWV VGGEF
//
