ID Q8ZV30_PYRAE Unreviewed; 626 AA.
AC Q8ZV30;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=acetate--CoA ligase {ECO:0000256|ARBA:ARBA00013275};
DE EC=6.2.1.1 {ECO:0000256|ARBA:ARBA00013275};
GN OrderedLocusNames=PAE2481 {ECO:0000313|EMBL:AAL64226.1};
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306 {ECO:0000313|EMBL:AAL64226.1, ECO:0000313|Proteomes:UP000002439};
RN [1] {ECO:0000313|EMBL:AAL64226.1, ECO:0000313|Proteomes:UP000002439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 /
RC IM2 {ECO:0000313|Proteomes:UP000002439};
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE009441; AAL64226.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8ZV30; -.
DR STRING; 178306.PAE2481; -.
DR EnsemblBacteria; AAL64226; AAL64226; PAE2481.
DR KEGG; pai:PAE2481; -.
DR PATRIC; fig|178306.9.peg.1850; -.
DR eggNOG; arCOG01529; Archaea.
DR HOGENOM; CLU_000022_3_6_2; -.
DR InParanoid; Q8ZV30; -.
DR Proteomes; UP000002439; Chromosome.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
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 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 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:UP000002439}.
FT DOMAIN 37..83
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 102..460
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 513..592
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 626 AA; 69789 MW; DA8376957A52A98F CRC64;
MELWRPEKHH LEESNVAKYI TSHGIKGLDD FLSLTFDKPE EFWRSFEKEV LKLGWYEEYI
KVLDLSKGVQ WPRWFVGGKI NIADQLEDSS RPLVKWEGED GSTAVWSYSE VLYKAKAVAS
WLKRNGLEKG DRVAIFMPMV PEIIPVMLGA IRAGGVIVPL FSGFGKEAIR VRLEDSEAKF
VFASDISYRR GKEIDMLSEL RAGLTPSVKR VVVQERSGRS SGYTPLSEVF KTGGDHVERA
DAEDPIMIIY TSGTTGKPKG TVHTHDGFPV KAAADVYFHF DVSEGETLSW VTDMGWMMGP
WMVFAAYLLR GSMAFFEGAP DYPKDRLWRF VERFKVNALG LAATLTRYLR SIGAAAEPGQ
LDSLKAFGNT GEPIDVESWL WLYRMGRGRI PIINYSGGTE ISGGILGCYV VRPIKPSSFN
GPSIGTKAAV FTEDGRPAPP GVEGELVVLS VWPGMTRGFW RDPQRYLETY WNKWPGVWAH
GDAAVVDEEG FFYILGRADD TIKVAGKRLG PAEIETVLNA HPAVAESACI GVPHEIKGEV
PVCFVVLKPG YEPSEALRRE LIKLTEEALG KAFGAVEDIR FVKMLPKTRN AKIMRRVIRA
VYLGRNPGDL SALENPEAIE EIKRAL
//
