ID D7B2W9_NOCDD Unreviewed; 685 AA.
AC D7B2W9;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Acetoacetyl-CoA synthase {ECO:0000313|EMBL:ADH68659.1};
GN OrderedLocusNames=Ndas_3253 {ECO:0000313|EMBL:ADH68659.1};
OS Nocardiopsis dassonvillei (strain ATCC 23218 / DSM 43111 / CIP 107115 / JCM
OS 7437 / KCTC 9190 / NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509)
OS (Actinomadura dassonvillei).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=446468 {ECO:0000313|EMBL:ADH68659.1, ECO:0000313|Proteomes:UP000002219};
RN [1] {ECO:0000313|EMBL:ADH68659.1, ECO:0000313|Proteomes:UP000002219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23218 / DSM 43111 / CIP 107115 / JCM 7437 / KCTC 9190 /
RC NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509
RC {ECO:0000313|Proteomes:UP000002219};
RX PubMed=21304737; DOI=10.4056/sigs.1363462;
RA Sun H., Lapidus A., Nolan M., Lucas S., Del Rio T.G., Tice H., Cheng J.F.,
RA Tapia R., Han C., Goodwin L., Pitluck S., Pagani I., Ivanova N.,
RA Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Djao O.D., Rohde M., Sikorski J.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Nocardiopsis dassonvillei type strain (IMRU
RT 509).";
RL Stand. Genomic Sci. 3:325-336(2010).
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DR EMBL; CP002040; ADH68659.1; -; Genomic_DNA.
DR RefSeq; WP_013154266.1; NC_014210.1.
DR AlphaFoldDB; D7B2W9; -.
DR STRING; 446468.Ndas_3253; -.
DR KEGG; nda:Ndas_3253; -.
DR eggNOG; COG0365; Bacteria.
DR HOGENOM; CLU_000022_3_3_11; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000002219; Chromosome 1.
DR GO; GO:0030729; F:acetoacetate-CoA ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR005914; Acac_CoA_synth.
DR InterPro; IPR032387; ACAS_N.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR NCBIfam; TIGR01217; ac_ac_CoA_syn; 1.
DR PANTHER; PTHR42921; ACETOACETYL-COA SYNTHETASE; 1.
DR PANTHER; PTHR42921:SF1; ACETOACETYL-COA SYNTHETASE; 1.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002219}.
FT DOMAIN 49..103
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 112..499
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 567..641
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 685 AA; 75112 MW; 6DE9CA131C166751 CRC64;
MTENSVPRVL WKPDEERAAS SNIVAFARWA EREKGVRAFG DASAASFDYD SLWRWSVTDV
DGFWESVWEY YGVRSETPYE RVLGERTMPG AEWFPGATLN YARHVFEGRD DDRVAIRHAT
ELRGLGEWTW GDLRRRTAAI AAGLRGLGVG PGDRVVAYLP NLPETVAAFY AAASLGAVWS
SCSPDFGVRS VIDRFAQIEP KVLLAVDGYR YGGKDFDRRP VVEELRAALP TVEHTVLLDY
LHPGEFLDGT LPWGRLEESG AGAELEFASV PFDHPLWVLY SSGTTGLPKA IVHGHGGILL
EQLKNLHLHL DAQEHDRVFW FTTTGWMMWN FLVSVLLTKA SIVLYDGSPA HPSPSTTLNV
RPSAAATPQP DLGALWDLAA EAGVTVFGTS AGFLSSCMKE GVHPRRGRDL SALKAIGSTG
SPLSPEAFSW VYEEFGEDLW LFSTSGGTDV CSCLVGGTPT LPVHEGEIQS RALGMAVASW
DPDGKELVNE VGELVVTEPA PSMPLFLWGD DSGERLRESY FSVYPGVWRH GDWIAITDRG
TAVIYGRSDS TINRGGVRMG TSEIYRAVLA LDEVVDALVV DVPQADGSSR IELFTVLREG
ADLEGDLPRE IARRIRTDCS PRHVPDRVRV IGAVPRTLSG KVLEVPVKRI LMGERPDRVA
SRDSLANPEA LDFFSTLAGE RENTG
//
