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Database: UniProt
Entry: K8GG52_9CYAN
LinkDB: K8GG52_9CYAN
Original site: K8GG52_9CYAN 
ID   K8GG52_9CYAN            Unreviewed;       925 AA.
AC   K8GG52;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=OsccyDRAFT_4211 {ECO:0000313|EMBL:EKQ67913.1};
OS   Leptolyngbyaceae cyanobacterium JSC-12.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae.
OX   NCBI_TaxID=864702 {ECO:0000313|EMBL:EKQ67913.1, ECO:0000313|Proteomes:UP000001332};
RN   [1] {ECO:0000313|EMBL:EKQ67913.1, ECO:0000313|Proteomes:UP000001332}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JSC-12 {ECO:0000313|EMBL:EKQ67913.1,
RC   ECO:0000313|Proteomes:UP000001332};
RG   DOE Joint Genome Institute;
RA   Brown I., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA   Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA   Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RT   "Improved high quality draft of Oscillatoriales sp. JSC-12.";
RL   Submitted (OCT-2012) 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:EKQ67913.1}.
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DR   EMBL; AJUB01000015; EKQ67913.1; -; Genomic_DNA.
DR   AlphaFoldDB; K8GG52; -.
DR   STRING; 864702.OsccyDRAFT_4211; -.
DR   PATRIC; fig|864702.5.peg.4508; -.
DR   eggNOG; COG0189; Bacteria.
DR   eggNOG; COG0769; Bacteria.
DR   HOGENOM; CLU_016806_0_0_3; -.
DR   Proteomes; UP000001332; 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; 3.30.470.20; 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   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001332}.
FT   DOMAIN          241..495
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   925 AA;  100486 MW;  EEF40A87FE7A6B69 CRC64;
     MSSGCLTTLK LFLITVVMKI LKIQTLRGPN YWSIRRQKLI VMRLDLEELA ETPSNQIQGF
     YEGLTNVLPT LIEHFCSPGC RGGFLKRVQE GTMMGHIVEH VALELQELAG MPVGFGRTRE
     TSTPGVYQVV IEYQYEQAGR YAARAAVRLC QSIVDTGNYP QEELEKDLED LRQLASDASL
     GPSTESIVKE AEAKGIPWLE LGARHLIQLG YGVHQKRMQA TLSNQTGILG VELASDKEGT
     KRVLGDAGIP VPRGTTINFL DELEEAIEYV GGYPIVIKPL DGNHGRGITI DINSWEEAVE
     AYDAAKAVSR SVIVERFYRG QDHRILVVNG RVVAVAERIP AHVVGDGRST IEELIDETNK
     DPRRGEGHDN VLTKIELDRT SWQLLDKQGY TLDTVLEAGQ ICYLRATANL STGGIAIDRT
     DDIHPENVWI AQRVAKTIGL DICGIDVVTP DITRPLREMD GVIVEVNAAP GFRMHVCPSV
     GIPRNVAEPV LEMLFPPGTP SRVPIIAITG TNGKTTTTRL IAHIFRQTGQ TVGYTTTDGT
     YIGDYLAEPG DNTGPQSAHL ILQDPTVEVA VLESARGGIL RSGLAFSACD VGVVLNVAAD
     HLGLGDIDTI EQMARVKSVV PETVMPNGYA VLNADDPLVA EMASRVNAQV AYFSMHPDSE
     LLRTHTQKGG LAAVYENGYL SILKGDWTLR IEQAANVPLT LGGRAPFMIA NALAASLAAF
     AQGVDIKDIR AALLTFKAST AQTPGRMNLF NLGKFHALVD YAHNAHSYEA LAGFVRNWPG
     ERIGVVGGPG DRRDEDFITL GTLSAEMFDR IIVKEDDDNR GRPRGDAARL IARGLQQAKP
     DCRYEAILDE TTAIQTALDS APLNSLVVIL PESVTRAIQL IEARRPISEP EVTPTTPMTT
     STTTVAETQV VAEVVDANQS SEVPA
//
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