ID D7B1U9_NOCDD Unreviewed; 597 AA.
AC D7B1U9;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Acyl-CoA synthetase {ECO:0000256|ARBA:ARBA00032875};
GN OrderedLocusNames=Ndas_1129 {ECO:0000313|EMBL:ADH66570.1};
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:ADH66570.1, ECO:0000313|Proteomes:UP000002219};
RN [1] {ECO:0000313|EMBL:ADH66570.1, 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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00024484};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC Evidence={ECO:0000256|ARBA:ARBA00024484};
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DR EMBL; CP002040; ADH66570.1; -; Genomic_DNA.
DR RefSeq; WP_013152177.1; NC_014210.1.
DR AlphaFoldDB; D7B1U9; -.
DR STRING; 446468.Ndas_1129; -.
DR KEGG; nda:Ndas_1129; -.
DR eggNOG; COG1022; Bacteria.
DR HOGENOM; CLU_000022_45_5_11; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000002219; Chromosome 1.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR CDD; cd05907; VL_LC_FACS_like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
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 PANTHER; PTHR43272:SF83; ACYL-COA SYNTHETASE LONG-CHAIN, ISOFORM J; 1.
DR PANTHER; PTHR43272; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:ADH66570.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002219}.
FT DOMAIN 13..423
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 597 AA; 64408 MW; 4F4CF8061A043C16 CRC64;
MPPTGRTLPS LLARNAADRP DAPALSWRAP DGGDWTTLTW SRVRDRVAAL AEGYAALGVG
PGDHVLLMMG NRPEHWLSDL ALVHAGAVPT TVYDTAASEQ VAHVARHSRA RLAVVGDTAT
ATAWEGLLAD PEVPLAALVV VDGADPDRGH TDYALLESTP AGTAFERWRD LTPDDLLTVV
YTSGTTGDPK GVAITHRDML ANATALDAAV ALPEHPDHVC YLPLAHIAER MLGLYLPVFR
ASHVWMCESL RDLPGVLRHV RPPQFFGVPR VWEKFASALR AGLARMPEET RAAVDAATAV
AAEHVAHRER GEEVPAELGE RFERARAEVL LPLLAQVGLD RVGWASSASA PMPLDVVRFW
AGFGIVVMDA WGLTESVGVA TVNSPATGFR LGSVGRPLAS VRVRVAEDGE VWLRGESVFG
GYLQPDGSVR PATDAEGWFA TGDVGRLDGD GYLWITDRKK ELIVTSQGKN VAPAPVENAL
KEHPIVGQAY VHGDRRPYLV ALLVPDRETL PVWAAARGID TGGDWEALVA HPEVAAEAER
AVAAANARFS RAEGVRRHRL LPGEWGPDTG ELTPSLKLRR RVVRERYADA LAELYRD
//
