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Database: UniProt
Entry: A0A094IDU1_9PEZI
LinkDB: A0A094IDU1_9PEZI
Original site: A0A094IDU1_9PEZI 
ID   A0A094IDU1_9PEZI        Unreviewed;      1116 AA.
AC   A0A094IDU1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=acetate--CoA ligase {ECO:0000256|ARBA:ARBA00013275};
DE            EC=6.2.1.1 {ECO:0000256|ARBA:ARBA00013275};
GN   ORFNames=V502_00259 {ECO:0000313|EMBL:KFZ25267.1};
OS   Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ25267.1, ECO:0000313|Proteomes:UP000029308};
RN   [1] {ECO:0000313|EMBL:KFZ25267.1, ECO:0000313|Proteomes:UP000029308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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:KFZ25267.1}.
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DR   EMBL; JPKE01000097; KFZ25267.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094IDU1; -.
DR   STRING; 1420915.A0A094IDU1; -.
DR   HOGENOM; CLU_281056_0_0_1; -.
DR   OrthoDB; 2419619at2759; -.
DR   Proteomes; UP000029308; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR   CDD; cd11061; CYP67-like; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 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   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_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   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029308};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        655..677
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        689..711
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          22..78
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          80..465
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          526..593
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   1116 AA;  125163 MW;  4338BB6F558AF654 CRC64;
     MSAYNVADEP DIDDIPKNIE EYRMIYEKSI KDPESFWAGK ARKLLDWYQD FKTIRTGNFR
     DGDNAWFQEG RLNASYNCID RHATHNPEKV AVVFEADEVN NGRKITYSQL LHDTCRLSYV
     LKDLGVKKGD IICIYLPNIY EALIAMLACS RIGAVHSVVF MGFSAAALRD RILDGRSKIV
     ITADEGRRGG KAVPTKAIVN EALLQCPLVT SCLVLKHTGS SVPWCPSRDV WWHEEARQWP
     AYIAPESMSA EDPLFLLYTS GSTGKPKGLM HTTAGFLLGA NITTKYVFGM QNTDVHFCAG
     DIGWITGHTY LVCGPLLVGA TTVVFEGTPA YPSFSRYWDI VEEHHVTHFY AAPTALRILK
     RAGDSHITVP MENLRVLGSI GEPIAPEVWK WYYETVGRKR AYIVDTYFQT ETGCHVISPL
     VGSIPTKPGC CTVPFLGIET VILDPILGHE LDGPAEGLLA IKRPWPSMAR TVWRAHERYM
     DTYFNEFPGY YFTGDGAFRD EDGYYWIRGR VDDVVNVSGH RLSTAEIEAS LLESPYVAES
     AAVGVKDEIS GQAVVAYISQ KDANTDAATI SAALIHQVRK DIGAFAAPKA FRIPKNPHPP
     HNRAHPLHSS AARGPCRFLL STAMNCLQSL TARAAAFAAG VATHAVGFRH GEWDLVTISL
     IWTFIVLHTS AIAALLYLSP GAAVTPLNAV SVVGALGLSS CLGIWTSMLV YRGFFHRLCR
     FQGPFLARFS NFYVTFLSAR RLHLYEEVYH LHKKYGDVVR LGPSELSISN ADAVTAIHGP
     QSKCTKGPWY NALHPRISLQ LIRDKSEHTR RRRVWDQGFS AKALREYEPR VTAYTDELLS
     HFSNSEGKPI NVTDWFNFYS FDVMGDLAWG KSFGMLQHGE KHYFMKSLHA DMKNVGLFSH
     LLWLFPIFKA VPILNYEHKR FWKWVHAQVN ERKEMTPDRP DVFSWLLEDF NSRKPTYQDE
     LNLNGDAYLI AVAGSDTTAA SLTCLFYQLS LHPECLSILQ KETDEGFEGS EGVDTALLGK
     LSYLNFVINE SLRLHPPVPS GVQRMTPPQG LTVGEMFIPG NTIVQIPSHT LYRDERYFER
     PDEFLPERWT THPELVKNAA VFAPFSTGKY RLGIGQ
//
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