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
//