ID Q5UXS1_HALMA Unreviewed; 652 AA.
AC Q5UXS1;
DT 07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 07-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=acetate--CoA ligase {ECO:0000256|ARBA:ARBA00013275};
DE EC=6.2.1.1 {ECO:0000256|ARBA:ARBA00013275};
GN Name=acs3 {ECO:0000313|EMBL:AAV47932.1};
GN OrderedLocusNames=rrnAC3230 {ECO:0000313|EMBL:AAV47932.1};
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569 {ECO:0000313|EMBL:AAV47932.1, ECO:0000313|Proteomes:UP000001169};
RN [1] {ECO:0000313|EMBL:AAV47932.1, ECO:0000313|Proteomes:UP000001169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809
RC {ECO:0000313|Proteomes:UP000001169};
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
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DR EMBL; AY596297; AAV47932.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5UXS1; -.
DR STRING; 272569.rrnAC3230; -.
DR PaxDb; 272569-rrnAC3230; -.
DR EnsemblBacteria; AAV47932; AAV47932; rrnAC3230.
DR KEGG; hma:rrnAC3230; -.
DR PATRIC; fig|272569.17.peg.3766; -.
DR eggNOG; arCOG04201; Archaea.
DR HOGENOM; CLU_000022_3_6_2; -.
DR Proteomes; UP000001169; Chromosome I.
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 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; 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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AAV47932.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001169}.
FT DOMAIN 40..92
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 95..478
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 538..615
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 652 AA; 71817 MW; B529D5E308E843C1 CRC64;
MYCQLMTRGD EPDRGQSQTG RETVEPPDWF VKQANVTDLA VYDRFEREWP DCWREAAELL
DWEKPFETVL RGTDGPPFEW FPDGRLNAAY NCLDRHLPER KNQLALVWEG HLGESRTYTY
LELYREVNAF AAALRDRGVG PDDVVTLYLP MVPELPVAML ACARLGVPHN VVFAGFSADA
LATRMERAES EYLITCDGYY RRGSAVAQKN KADNARITVD HDVSVVVLDR LGRDVHLGDD
YVDYHDLLAA HEGAEVEPVS QAADDPLFRI YTSGTTGQPK AVTHTTGGYL AHVAWTARSV
LDIKPEDTYW CSADIGWITG HSYIVYGPLA LGTTTVLYNG TADHPEKDRL WELIEKYAVD
VFYTAPTAVR AFMKWGEQYP EQHDLSSLRL LGTVGEPMDA HAWEWYREHI GGGECPVVDT
WWQTETGAIL VSTLPGVDEM KPGAAGTPLP GIEASVVTRS GATAEPNTAG ELVVTRPWPG
MPRALLDGTG WGSAPDSAEE WRYYPEDSVS VDADGYITFL GRIDDAINVA GRRFSTKELE
STVAGVTGVA EAAVVGADDE TTGTAVYVFA SPEDGYAESE LQTAIEDAIV NAIGGIARPK
EVVFTPDLPK TRSGKVMRRL LTSVANDEDL GDTSALRNPE ILGEIQSTTR RK
//
