ID A0A135URZ7_9PEZI Unreviewed; 662 AA.
AC A0A135URZ7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|RuleBase:RU361147};
DE EC=6.2.1.1 {ECO:0000256|RuleBase:RU361147};
GN ORFNames=CNYM01_08028 {ECO:0000313|EMBL:KXH63180.1};
OS Colletotrichum nymphaeae SA-01.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1460502 {ECO:0000313|EMBL:KXH63180.1, ECO:0000313|Proteomes:UP000070054};
RN [1] {ECO:0000313|EMBL:KXH63180.1, ECO:0000313|Proteomes:UP000070054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA-01 {ECO:0000313|EMBL:KXH63180.1,
RC ECO:0000313|Proteomes:UP000070054};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum nymphaeae SA-01.";
RL Submitted (FEB-2014) 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|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:KXH63180.1}.
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DR EMBL; JEMN01000224; KXH63180.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135URZ7; -.
DR Proteomes; UP000070054; 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}.
FT DOMAIN 36..92
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 94..479
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 541..619
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 662 AA; 73165 MW; 047F13B81307F690 CRC64;
MTDAAEPQKA PVVAEAHLVD TFQHPSKPHL SSLEDYQKLY KESITDPKAF WGTKARELLS
WFSDFQTVYS GSLAGGDSAW FVEGQLNACY NCVDRHAFKD PNRVAIIYEA DEPGEGRNVT
YGELLREVSR TAWVLKQMGV RKGDTVAIYL PMIPEAIIAL LACVRIGAVH SVVFAGFSAD
SLRDRVIDGN SKVVITTDEG KRGGKLIGTK KIVDDALKQC PDVSHVLVYK RTGADVPMTK
GRDWWWHEEV ENWPSYFPPE RVNSEDPLFL LYTSGSTGKP KGVMHTTGGY LVGAAATGKY
VFDIHDGDRY FCAGDVGWIT GHTYVVYAPL LLGVSTVVFE GTPAYPNFSR YWDIIANHQV
TQFYVAPTAL RLLKRAGDQH VKGDMKHLRV LGSVGEPIAA EVWKWYFEVV GKEEAHIVDT
YWQTETGSNV ITPLAGVTPT KPGSASLPFF GIEPSIIDPV SGEEIHGNDV EGVLAFKQAW
PSMARTVWGA HKRYMDTYLN VYPGYYFTGD GAGRDHEGFY WIRGRVDDVV NVSGHRLSTA
EIEAALIEHH SIAEAAVVGV ADELTGQAVN AFVALKDGNE ASDALRKEFI MQVRKSIGPF
AAPKAVHIVP DLPKTRSGKI MRRILRKILA GEEDQLGDVT TLSDPSIVEK IINIVHEEKR
KK
//