ID A0A1V0AHY1_9ACTN Unreviewed; 696 AA.
AC A0A1V0AHY1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Carboxylate--amine ligase {ECO:0000313|EMBL:AQZ69692.1};
GN ORFNames=BKM31_56840 {ECO:0000313|EMBL:AQZ69692.1};
OS Nonomuraea sp. ATCC 55076.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=1909395 {ECO:0000313|EMBL:AQZ69692.1, ECO:0000313|Proteomes:UP000190797};
RN [1] {ECO:0000313|Proteomes:UP000190797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55076 {ECO:0000313|Proteomes:UP000190797};
RX PubMed=28626548; DOI=10.1039/c6md00637j;
RA Nazari B., Forneris C.C., Gibson M.I., Moon K., Schramma K.R.,
RA Seyedsayamdost M.R.;
RT "Nonomuraea sp. ATCC 55076 harbours the largest actinomycete chromosome to
RT date and the kistamicin biosynthetic gene cluster.";
RL Med. Chem. Commun. 8:780-788(2017).
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DR EMBL; CP017717; AQZ69692.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V0AHY1; -.
DR STRING; 1909395.BKM31_56840; -.
DR KEGG; noa:BKM31_56840; -.
DR Proteomes; UP000190797; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 2.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032875; Succ_CoA_lig_flav_dom.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR PANTHER; PTHR43334; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR PANTHER; PTHR43334:SF1; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR Pfam; PF13549; ATP-grasp_5; 1.
DR Pfam; PF13380; CoA_binding_2; 1.
DR Pfam; PF13607; Succ_CoA_lig; 1.
DR SMART; SM00881; CoA_binding; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ligase {ECO:0000313|EMBL:AQZ69692.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000190797}.
FT DOMAIN 495..538
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 696 AA; 71867 MW; 7CD9191423A95C1F CRC64;
MTYMSVGELF NPRSIALVGA TDKSGWSIST LANLRAHGFP GPVHLVNPRG GVVHGQAAYR
SLTEIPERVD LAYVMVPTAA VLGVLREGAK LGIRCYVILT AGFGESGEEG ARLEAEITAF
AAEHGLTILG PNGNGYINAA AGVTPYGLPI QPPLLRGAVG VVLQSGALAS SVLGFAQARN
VGISLLTSMG NESVMTVTDV IEYLVDDPAT KVIALFLETV RNPAEFSRVA RRALEAGKPI
VALKIGRSKL ASHTAQAHTG ALVGDDDVID AALRQLGVIR VRSLEDLIIT AGLLASTGPL
PGRRVGVVTP SGGASEIIAD RAEDEGLELP PFAPETVAKL AEIVPSFGTV QNPLDVTGYV
LIDRTLLGRA LEAVTSDPGI DLIMLLSEPP KVAPPDPAPV LAMYAASAQR IAASPVPVVV
VSNVLTDVTE FGRRVQEETG FPYVAGGIEH GLQAIAAAVR WSEQRERVLA RPAPLPRAGA
APEGASGVWA EHRAAALLAA AGLPVVPSEL AGDEDAAVAA AGRFGYPVVL KAAAEGLGHK
SDVGGVRLGL GGAEEVRRAY REIVAAVPSL AGVLVQPQRT GGIELLVGVV RDAAWGLTLA
VGLGGVWVEV LRDTALRVLP VDAGEVRRAL GELRGAALLN GVRGGEPADL DAVADVVARV
AAFAESLGDG LESLEINPLL VSGSRVEALD ALITWR
//
