ID G0RZW2_CHATD Unreviewed; 1034 AA.
AC G0RZW2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=acetate--CoA ligase {ECO:0000256|ARBA:ARBA00013275};
DE EC=6.2.1.1 {ECO:0000256|ARBA:ARBA00013275};
GN ORFNames=CTHT_0004420 {ECO:0000313|EMBL:EGS23740.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS23740.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; GL988032; EGS23740.1; -; Genomic_DNA.
DR RefSeq; XP_006690982.1; XM_006690919.1.
DR AlphaFoldDB; G0RZW2; -.
DR STRING; 759272.G0RZW2; -.
DR GeneID; 18254480; -.
DR KEGG; cthr:CTHT_0004420; -.
DR eggNOG; KOG1175; Eukaryota.
DR HOGENOM; CLU_293724_0_0_1; -.
DR OMA; AIKASWP; -.
DR OrthoDB; 144557at2759; -.
DR Proteomes; UP000008066; 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: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};
KW Ligase {ECO:0000256|ARBA:ARBA00022598}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008066};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 136..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 408..464
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 466..856
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 914..992
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1034 AA; 112628 MW; 93277FA1F809B16F CRC64;
MQEYIVAGWH SEDPAEAKQG SGLQKSQRLS GLVPKSALWA TPPDTMGPGF PPRAWPCRGE
TGRSSPTLVK EEGGLGQAQG CWKTEPEIGS QGIGTDQRRS RHKAQGTANS NAGTGDAMGV
CRTEGKLTRA GRAASLPTYV VVLGATVIIP AGCYSITSVI AANLHREGES PPDHGTSSCV
ASAASVTHAG SASRWPKRPN LAGMPLVRVD VGHHTPHTPH THAHTPSASS VSVSASASAG
CWLWLLQKPR SRPVAPLVLT FPLSPLATAL VANFFFASRW SSSLTSPAPH PSLSPSSTCA
RRISRRRCCG CRCRFSTFPG NPTLFCANTL ADSSRSLPRH RAPPSLSLSQ QPRHIRTLQT
LSTTPKMSQG SPKAPVVAEA HEVDTYHPPK KMFAKHPSKP HLSGLEEYQK LYKESITQPD
KFWGRLAREL LTWHRDFQTV RSGSLVNGDV AWFLEGEINA SYNCVDRHAF ADPNRVAIIY
EADEPTDGRS VTYGELLREV SRVAHVLKAM GVRKGDTVAI YLPMIPEAVV ALMACARIGA
IHSVVFAGFS ADSLRDRVLD ARCKVVITTD EGKRGGKLIG TKKIVDEALK QCPEVKHVLV
YKRTGADIPM TPGRDLWWHE EVQKYPNYIP PEPMNSEDPL FLLYTSGSTG KPKGVMHTTG
GYLVGAAATG KYVFDIHPGD RYFCGGDVGW ITGHTYVVYA PLLLGVTTVV FEGTPAYPNF
SRYWDIIEKH GVTQFYVAPT ALRLLKRAGD QFVKGDFNKH LRVLGSVGEP IAAEVWKWYF
EVVGKEEAQV VDTYWQTETG SHVIAPLAGV TPTKPGSASL PFFGIEPAII DPVSGEEIHG
NDVEGVLAFK QPWPSMARTV WGAHKRYMET YLNVYKGYYF TGDGAGRDHE GFYWIRGRVD
DVVNVSGHRL STAEIEAALI EHPIIAEAAV VGVADELTGQ AVNAFVSIKE GHEASDALRK
EFILQVRRSI GPFAAPKAVY IVPDLPKTRS GKIMRRILRK VLAGEEDQLG DVTTLSDPSV
VGRIIDVVRE ARRK
//
