ID A0A139HM21_9PEZI Unreviewed; 750 AA.
AC A0A139HM21;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|RuleBase:RU361147};
DE EC=6.2.1.1 {ECO:0000256|RuleBase:RU361147};
DE Flags: Fragment;
GN ORFNames=AC579_7269 {ECO:0000313|EMBL:KXT03409.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT03409.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXT03409.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT03409.1,
RC ECO:0000313|Proteomes:UP000073492};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) 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:KXT03409.1}.
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DR EMBL; LFZO01000607; KXT03409.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139HM21; -.
DR STRING; 113226.A0A139HM21; -.
DR Proteomes; UP000073492; 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:UP000073492}.
FT DOMAIN 124..180
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 182..567
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 629..707
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KXT03409.1"
FT NON_TER 750
FT /evidence="ECO:0000313|EMBL:KXT03409.1"
SQ SEQUENCE 750 AA; 82837 MW; 1754C77B1EE6173E CRC64;
IGFSAAPRRP ATTLTHDSDF STTNNTSEAW LESSSAVYIA TPFLSSRSLA DHCILTARHT
AHRTLPTAHC IHPLTEYRTP NMSEGAQQPP NGIPESHSAD TYHVPDAFLG KHPAKPHIES
LDKYKEMYKE SITNPDHFWG KLARELLTWE KDFHTVHTGT LAGGDNAWFL EGKLNASYNC
VDRHAAKNPH KPAIIYEADE ASDGRTITYA ELLREVSKLS WVLKQMGVKK GDTVALYLPM
IPEAIVAFLA CTRIGAVHSV VFAGFSADSL RDRILDAQSK VVITTDEGKR GGKTIGTKKI
VDEALKQCPD VTNCLVYKRT GVDVPWTKGR DLWWHEETEK WPAYFAPESM SSEDPLFLLY
TSGSTGKPKG VMHTTAGYLL GAAATGKYVF DIHDSDKFFC GGDVGWITGH TYVVYAPLVL
GVATVVFEGT PAYPDFSRYW EVCEKHQVTQ FYVAPTALRL LKRAGDQHVK HQMKSLRVLG
SVGEPIAAEV WKWYHEIVGK KEAHVVDTYW QTETGSHVIT PLGGVTPTKP GSASLPFFGI
EPAIIDPVSG EEIQGNDVEG VLAFKQAWPS MARTVWGAHK RYMDTYLNVY KGYYFTGDGA
ARDYEGYYWI RGRVDDVVNV SGHRLSTAEI EAALIEHHAV GEAAVVGVND ELTGQAVNAF
VSIKDGNEIN DQLKKDLVLQ VRKSIGPFAA PKAIYTIPDL PKTRSGKIMR RILRKILAGE
EDQLGDTSTL ADPSVVDKII QTVHESKPTK
//
