ID F4B998_ACIHW Unreviewed; 646 AA.
AC F4B998;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Acetate-CoA ligase {ECO:0000313|EMBL:AEE93891.1};
GN OrderedLocusNames=Ahos_1005 {ECO:0000313|EMBL:AEE93891.1};
OS Acidianus hospitalis (strain W1).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Acidianus.
OX NCBI_TaxID=933801 {ECO:0000313|EMBL:AEE93891.1, ECO:0000313|Proteomes:UP000008458};
RN [1] {ECO:0000313|EMBL:AEE93891.1, ECO:0000313|Proteomes:UP000008458}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W1 {ECO:0000313|EMBL:AEE93891.1,
RC ECO:0000313|Proteomes:UP000008458};
RX PubMed=21607549; DOI=10.1007/s00792-011-0379-y;
RA You X.Y., Liu C., Wang S.Y., Jiang C.Y., Shah S.A., Prangishvili D.,
RA She Q., Liu S.J., Garrett R.A.;
RT "Genomic analysis of Acidianus hospitalis W1 a host for studying
RT crenarchaeal virus and plasmid life cycles.";
RL Extremophiles 15:487-497(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=W1;
RA You X.Y., Liu C., Wang S.Y., Jiang C.Y., Shah S.A., Prangishvili D.,
RA Liu S.J., Garrett R.A.;
RT "Genomic analyses of Acidianus hospitalis W1 a host for studying
RT crenarchaeal virus and plasmid life cycles.";
RL Extremophiles 0:0-0(2011).
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DR EMBL; CP002535; AEE93891.1; -; Genomic_DNA.
DR RefSeq; WP_013775807.1; NC_015518.1.
DR AlphaFoldDB; F4B998; -.
DR STRING; 933801.Ahos_1005; -.
DR GeneID; 10600478; -.
DR KEGG; aho:Ahos_1005; -.
DR eggNOG; arCOG01529; Archaea.
DR HOGENOM; CLU_000022_3_6_2; -.
DR OrthoDB; 371752at2157; -.
DR Proteomes; UP000008458; Chromosome.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IEA:InterPro.
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:SF232; ACETYL-COENZYME A SYNTHETASE; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AEE93891.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 16..70
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 71..458
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 519..597
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 646 AA; 73618 MW; 1C7BCE3097A5F2CF CRC64;
MSENLPFEER YYQPPYKQLY KQSLEEPEKF WREMAEGLEW FSPFDKVLDE SNAPFYRWFV
GGKINITYNA LDRQVKVRRN KIAIYWENEK GESRQLTYGE LYNEVNRFAK ILQDLGIKKG
DRVLIYLPLM PELPIAMLAC ARIGAVHSVV FSGFSTQAVI DRINDAKAKL VITTSHTMRR
GKRVELKRII DEAVSQTPSV EKVLVIKRDE EIELNEERDV LYQDLIKRTG YKKVEPEETL
STDPLFILYT SGTTGKPKGI LHLHGGYGLW TYLTTQWVFD LRDTDVFFNT ADIGWITGHS
YIVYGPLQNG ASVLMYEGVP DYPNPDRWWE LVEKYGVTVF YTSPTAIRSL MKYGEEWVKK
HDLSTLRILG SVGEPINPEA WRWYFKNVGN SSLPIVDTWW QTETGGIMIS ATPGLGNYLL
KPSANGLPLP GVDADVFTED GKQAKPREKG YIVIKRPWPG MLAGVWGDPE RYVKTYFSKF
PGVYYPGDYA VRDEEGFFYI LGRADEVLKI AGHRIGTREI EDILISHPAV AESAVIGVPD
PVRGEVAVAA IVLKQGYQPS EELRKSLIEY VKNNLGPIVI FGGLYFVSKL PKTRSGKIMR
RVVRSVISGQ PLGDVSTLED ETSVDELKKV IEEFTKEIQG QQNEKK
//
