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Database: UniProt
Entry: A0A024GHN5_9STRA
LinkDB: A0A024GHN5_9STRA
Original site: A0A024GHN5_9STRA 
ID   A0A024GHN5_9STRA        Unreviewed;       659 AA.
AC   A0A024GHN5;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|RuleBase:RU361147};
DE            EC=6.2.1.1 {ECO:0000256|RuleBase:RU361147};
GN   ORFNames=BN9_069390 {ECO:0000313|EMBL:CCI46011.1};
OS   Albugo candida.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI46011.1, ECO:0000313|Proteomes:UP000053237};
RN   [1] {ECO:0000313|EMBL:CCI46011.1, ECO:0000313|Proteomes:UP000053237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI46011.1,
RC   ECO:0000313|Proteomes:UP000053237};
RA   Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA   Jones J.D.G.;
RT   "Recombination and specialization in a pathogen metapopulation.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:456215; EC=6.2.1.1;
CC         Evidence={ECO:0000256|RuleBase:RU361147};
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|RuleBase:RU361147}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCI46011.1}.
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DR   EMBL; CAIX01000115; CCI46011.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024GHN5; -.
DR   STRING; 65357.A0A024GHN5; -.
DR   InParanoid; A0A024GHN5; -.
DR   OrthoDB; 144557at2759; -.
DR   Proteomes; UP000053237; Unassembled WGS sequence.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR   CDD; cd05966; ACS; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR011904; Ac_CoA_lig.
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; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR   PANTHER; PTHR24095; ACETYL-COENZYME A SYNTHETASE; 1.
DR   PANTHER; PTHR24095:SF14; ACETYL-COENZYME A SYNTHETASE 1; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361147};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU361147};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361147};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053237}.
FT   DOMAIN          24..80
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          87..477
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          538..616
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   659 AA;  73179 MW;  9AC599E19ADC9609 CRC64;
     MATEVFPVIK RAAPQAHING PEHYDQLYKD SIENPDEFWG SCARKHLSWF HPFDHVSSGS
     LASGDVAWFL NGKLNVSYNC IDRHVLKGKD EKTAIIWEAD DIGTGRSISF RELLRETCRV
     ANLMKHFGVR KGDTVAIYMP MIPEIASVML ACTRIGAVHS VVFAGFSSDS LRDRIQDARC
     KVFRCVCQWI FTSDEGKRGG RILPLKQVVD RAISGLDFVE NVFVFRRTNN PNIPIVPPKD
     VDMTINLSRF RPYCPAEWMD SEDLLFILYT SGSTGSPKGV AHSTAGYLLY SMLTAKYTFD
     LQENDVFGCM ADCGWITGHT YNIYGTLCNG TTTVLFESTP MFPDHCRYWD LIQRHRVTKF
     YTAPTAIRSL MACGSDNIKD YDLSSLKVLG SVGEPINPEA WKWYFDVVGK GSCYITDTYW
     QTETGGHVGV GLPGVTLMKP GSCGKPFFGI EFVLIDSNGN ILEENDVEGQ LFIKKPWPGL
     ARTVYGDHWR YQSVYMTSHN GFYFTGDGAK RDKDGYYSIT GRIDDVLSTS GHRIGTAEVE
     GALATHNIVA EAAVVGVPHA IKGEGICCYV VLVGASKPSI EVTTELMQQV RIAIGPFATP
     DLIVYPSALP KTRSGKIIRR LLRKIAAGEE GQLGDTSTMV NAEIVPELIQ CFRDAVQKK
//
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