ID A0A239F6P6_9ACTN Unreviewed; 879 AA.
AC A0A239F6P6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Cyanophycin synthetase {ECO:0000313|EMBL:SNS52467.1};
GN ORFNames=SAMN06265355_119127 {ECO:0000313|EMBL:SNS52467.1};
OS Actinomadura mexicana.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=134959 {ECO:0000313|EMBL:SNS52467.1, ECO:0000313|Proteomes:UP000198420};
RN [1] {ECO:0000313|EMBL:SNS52467.1, ECO:0000313|Proteomes:UP000198420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44485 {ECO:0000313|EMBL:SNS52467.1,
RC ECO:0000313|Proteomes:UP000198420};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FZNP01000019; SNS52467.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239F6P6; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000198420; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IPR036565; Mur-like_cat_sf.
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; 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 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 224..479
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 879 AA; 91646 MW; 4CDC651D99EB3568 CRC64;
MRLDHVRRLG GPNVYLSRPV AIARLNLQGL TGHETTDHPG FAERLVDALP GLADHHCSAG
RPGGLLEAMA RGTYFGHVTE HVTLELSGLI GREVFFGRTV RAGGPAEYDV ILECPPDEPS
ASPVVERLIT LAVRIVNGAL AGLVPGTSAD LARVAAVHEE ERLGVSTAAL ARAARERGVP
VRRVGGLNLL RLGYGRYRRT VWAAMTDATS AIGMEVAGDK RLAHRLLADA GLPVPEGRVA
ASPGEALEAL RAVGGPVVVK PLAGHQGEGV HIELTTAPEV VAAFAAAAAG GGEVLVESYV
PGKDYRVLVV GGRVAAAAEL TAACVTGDGT APVAALMERV NADPARGEGH DRPLTRLVLG
PTELALLERQ GHGPRSVPAD GERVWLRRNA NLSTGGTSRD VTADVHPEVA AMCVRAAAAV
GMDVCGIDLR LPDAASPPPA EHGAAGILEV NAAPGLRMHL APHRGAGRDV AGDIIGLMYP
EGTPSRVPVV SVTGTNGKTT TVRMIAHMLE LDGRRTGMTS TEGVYVGGRL VHRSDASGPR
SAEMVLGDRS VEAAVLETAR GGIVRRGLGY DRADVAVVTN VTRDHLGVDD TESVDDLVDI
KALVAEEIRR GGHVVLNAED EASAGLAERP GVRERDPVLR YFALSPDAPV LAGHLRRGGA
GYSVRDGWLT EARGDRRTPI LPAAEVAGSF GGHARHVIAN ALAASAAARA LGVPVEVVAR
ALRSFDPHTR NPGRGCVYQV GANPVLVDYA HNPAAVGAMG AFVERCWGGA GVAAVTLPGD
RSDELVSETA RALAGTFGRV VVYEDEDLRG RRSGEMTRLI VQGLREVRPD VRHHPAGDLK
GALASALDMA APGEPVLLLY EKLQPVTELL ETLGGEPAG
//
