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Database: UniProt
Entry: Q2W9U1_MAGSA
LinkDB: Q2W9U1_MAGSA
Original site: Q2W9U1_MAGSA 
ID   Q2W9U1_MAGSA            Unreviewed;       652 AA.
AC   Q2W9U1;
DT   10-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   10-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   SubName: Full=Acyl-coenzyme A synthetase/AMP-(Fatty) acid ligase {ECO:0000313|EMBL:BAE49384.1};
GN   OrderedLocusNames=amb0580 {ECO:0000313|EMBL:BAE49384.1};
OS   Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Magnetospirillaceae; Paramagnetospirillum.
OX   NCBI_TaxID=342108 {ECO:0000313|EMBL:BAE49384.1, ECO:0000313|Proteomes:UP000007058};
RN   [1] {ECO:0000313|EMBL:BAE49384.1, ECO:0000313|Proteomes:UP000007058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMB-1 / ATCC 700264 {ECO:0000313|Proteomes:UP000007058};
RX   PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA   Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT   "Complete genome sequence of the facultative anaerobic magnetotactic
RT   bacterium Magnetospirillum sp. strain AMB-1.";
RL   DNA Res. 12:157-166(2005).
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DR   EMBL; AP007255; BAE49384.1; -; Genomic_DNA.
DR   RefSeq; WP_011383023.1; NC_007626.1.
DR   AlphaFoldDB; Q2W9U1; -.
DR   STRING; 342108.amb0580; -.
DR   KEGG; mag:amb0580; -.
DR   HOGENOM; CLU_000022_3_3_5; -.
DR   OrthoDB; 4471305at2; -.
DR   Proteomes; UP000007058; Chromosome.
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   CDD; cd05943; AACS; 1.
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   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:BAE49384.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007058}.
FT   DOMAIN          36..93
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          103..469
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          545..614
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   652 AA;  71393 MW;  69334E27CCEE2A48 CRC64;
     MSVLLWQPSK ERAEASALAR FMRRADARFQ VGATDYAGLW RWSVDRPDQF WSLVWDEVGI
     IGDRPDGGVV VDDAGRMPGA RWFPEARLNF AENLLRRDDG GDALVFWGED KVKRRLSFAE
     LRALVSRLQQ ALSAAGVGKG DRVAGYMPNM PESVAFMLAV ASLGAIWSSA SPDFGVQGVL
     DRFGQIAPKV LVAAEGYFYS GKAHDCLEKL AAIVPGIPSL ERVVVVPYTR EAADLSGVDK
     AVHLGDFLAP FPAKAVEFLR LPFDHPLYIM YSSGTTGAPK CIVHSAGGSL IQQLKEHRLH
     CDVRKDDRVF YFTTCGWMMW NWLVAGLGAE ATLLLYDGNP SHLGGNILFD FADAEGMTLF
     GTSAKWIDAI AKSGLEPIKT HSLATVRTIC STGSVLAPEG FDYVYAKVKA DVQLASISGG
     TDIISCFMLG NPLVPVYRGE IQCRGLGMKV EVFDENGQSL AGSKGELVCT RAFPSMPVGF
     WNDDDGAKYR AAYFEKFPGI WTHGDWVELN PETGGIIVFG RSDATLNPGG VRIGTAEIYR
     QVEQIDDVLE SLVIGQDWQA DVRVVLFVRL RDGVTLSPEL ETRIKKRIRD NTTPRHVPAK
     VVQVADIPRT KSGKIVELAV RDVVHGRAVK NKEALANPEA LDLFAGRAEL EE
//
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