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Database: UniProt
Entry: N4VVD6_COLOR
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Original site: N4VVD6_COLOR 
ID   N4VVD6_COLOR            Unreviewed;       670 AA.
AC   N4VVD6;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|RuleBase:RU361147};
DE            EC=6.2.1.1 {ECO:0000256|RuleBase:RU361147};
GN   Name=acu-5 {ECO:0000313|EMBL:TDZ23390.1};
GN   ORFNames=Cob_v003855 {ECO:0000313|EMBL:TDZ23390.1};
OS   Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS
OS   414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum
OS   lagenarium).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum orbiculare species complex.
OX   NCBI_TaxID=1213857 {ECO:0000313|EMBL:TDZ23390.1, ECO:0000313|Proteomes:UP000014480};
RN   [1] {ECO:0000313|Proteomes:UP000014480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC   {ECO:0000313|Proteomes:UP000014480};
RX   PubMed=23252678; DOI=10.1111/nph.12085;
RA   Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA   Takano Y., Kubo Y., Shirasu K.;
RT   "Comparative genomic and transcriptomic analyses reveal the hemibiotrophic
RT   stage shift of Colletotrichum fungi.";
RL   New Phytol. 197:1236-1249(2013).
RN   [2] {ECO:0000313|Proteomes:UP000014480}
RP   GENOME REANNOTATION.
RC   STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC   {ECO:0000313|Proteomes:UP000014480};
RX   PubMed=30893003; DOI=10.1094/MPMI-12-18-0352-A;
RA   Gan P., Tsushima A., Narusaka M., Narusaka Y., Takano Y., Kubo Y.,
RA   Shirasu K.;
RT   "Genome sequence resources for four phytopathogenic fungi from the
RT   Colletotrichum orbiculare species complex.";
RL   Mol. Plant Microbe Interact. 32:1088-1090(2019).
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|ARBA:ARBA00006432, 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:TDZ23390.1}.
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DR   EMBL; AMCV02000006; TDZ23390.1; -; Genomic_DNA.
DR   AlphaFoldDB; N4VVD6; -.
DR   STRING; 1213857.N4VVD6; -.
DR   EnsemblFungi; ENH87937; ENH87937; Cob_04109.
DR   eggNOG; KOG1175; Eukaryota.
DR   HOGENOM; CLU_000022_3_6_1; -.
DR   OrthoDB; 144557at2759; -.
DR   Proteomes; UP000014480; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
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:UP000014480}.
FT   DOMAIN          44..100
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          102..487
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          549..627
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   670 AA;  74118 MW;  AF4D2B19C91D5436 CRC64;
     MAASTEQQKA PVVAEAHLVD TFHPPQKMLD KHPSKPHLSS LEDYQKLYKE SITDPKAFWG
     TKARELLSWF TDFQTVYSGS LENGDSAWFA EGELNASYNC VDRHAFKDPN RVAIIYEADE
     AGEGRNVTYG ELLREVSKTA WVLKQMGVRK GDTVAIYLPM IPEALVALLA CSRIGAVHSV
     VFAGFSADSL RDRVLDGNSK VVITTDEGKR GGKLIGTKKI VDDALKQCPD VSHVLVYKRT
     GADVPMTKGR DWWWHEEVEK WPAYYPPERV SSEDPLFLLY TSGSTGKPKG VLHTTGGYLV
     GAAATGKYVF DIHDGDRYFC GGDVGWITGH TYVVYAPLLL GVTTVVFEGT PAYPNFSRYW
     DIIAEHQITQ FYVAPTALRL LKRAGDQHVK GDMKHLRVLG SVGEPIAAEV WKWYFEVVGK
     EEAHIVDTYW QTETGSNVIT PLAGVTPTKP GSASLPFFGI EPAIIDPVSG EEIHGNDVEG
     VLAFKQAWPS MARTVWGAHK RYMDTYLNVY KGYYFTGDGA GRDHEGFYWI RGRVDDVVNV
     SGHRLSTAEI EAALIEHHAI AEAAVVGVAD ELTGQAVNAF VAIKDGNEAT DALRKEFIMQ
     VRKSIGPFAA PKAVHIVPDL PKTRSGKIMR RILRKILAGE EDQLGDVTTL SDPSIVEKII
     NVVHEEKRKK
//
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