ID A0A150V6V0_9PEZI Unreviewed; 707 AA.
AC A0A150V6V0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=AMP-dependent synthetase/ligase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=M433DRAFT_65523 {ECO:0000313|EMBL:KYG46258.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG46258.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG46258.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG46258.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
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:KYG46258.1}.
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DR EMBL; JPDO01000123; KYG46258.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150V6V0; -.
DR STRING; 766039.A0A150V6V0; -.
DR Proteomes; UP000075602; Unassembled WGS sequence.
DR GO; GO:0030729; F:acetoacetate-CoA ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd05943; AACS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR005914; Acac_CoA_synth.
DR InterPro; IPR032387; ACAS_N.
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; TIGR01217; ac_ac_CoA_syn; 1.
DR PANTHER; PTHR42921; ACETOACETYL-COA SYNTHETASE; 1.
DR PANTHER; PTHR42921:SF1; ACETOACETYL-COA SYNTHETASE; 1.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000075602}.
FT DOMAIN 46..103
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 121..504
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 707 AA; 78961 MW; 6A21BE2CB22DF9F8 CRC64;
MAANSNDSNG TDERKLLWRH PSPKDTFMWS FLQTVNEQHK QSFSSYDELY QWSIRDIDQF
WEDVWNFCGI RAKRPFQKVV SDTVTMFPRP SWFDGALLNF AENLLFPVLP GEKRVDESSI
AVIAATETSR EYVTWKELRE RVRQCQSGML AMGLQTGDRV AGYVANHTNA LVAMLAASSL
GAIWTAVSPD TGVTAVLDRM IQVKPTLLFT DNAVMYNAKT HPVLPKVKEI LQSLPTVKAT
IIFDTAPGIA SVIEGVSQEL ASQLFTYSKF TALNPSSSGE LHFKQLPPDH PVYILYSSGT
TGAPKCIVHG AIGTLIQHKK EHILQADIRP GDRLFYFTTC TWMMWHWLVS GLASGATVVL
YDGSPFQYRN DKGMSVKDDL AMPKLVDEIG ISQFGTSAKY LSVLEQKNIM PKDHNLTLKT
LKAIYSTGSP LAPSTFEYVY KAFGQVNLGS ITGGTDIISL FGAPCPLHPV YIGEIQVLGL
GMAVQAWDYT GKDISKSGEP GDLVCVKPFP CQPVLFWSAK GKEEGDSKYR SSYFEHFKGV
WHHGDFIRFN PETGGLIMLG RSDGVLKPSG VRFGSAEIYN VLLKYFPEQV EDALCIGRRR
ENDMDETVVL FLKMKEHIPF TSELVDDVKM RIRKELSARH VPGIVDETPE IPHTTNGKKV
EGAVKQILCG MNVKTSASVA NADCLEWYRN WARDHNDREE TQINPVN
//
