ID   C8X4E2_DESRD            Unreviewed;       661 AA.
AC   C8X4E2;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|HAMAP-Rule:MF_01123};
DE            Short=AcCoA synthetase {ECO:0000256|HAMAP-Rule:MF_01123};
DE            Short=Acs {ECO:0000256|HAMAP-Rule:MF_01123};
DE            EC=6.2.1.1 {ECO:0000256|HAMAP-Rule:MF_01123};
DE   AltName: Full=Acetate--CoA ligase {ECO:0000256|HAMAP-Rule:MF_01123};
DE   AltName: Full=Acyl-activating enzyme {ECO:0000256|HAMAP-Rule:MF_01123};
GN   Name=acsA {ECO:0000256|HAMAP-Rule:MF_01123};
GN   OrderedLocusNames=Dret_2132 {ECO:0000313|EMBL:ACV69416.1};
OS   Desulfohalobium retbaense (strain ATCC 49708 / DSM 5692 / JCM 16813 /
OS   HR100).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfohalobiaceae; Desulfohalobium.
OX   NCBI_TaxID=485915 {ECO:0000313|EMBL:ACV69416.1, ECO:0000313|Proteomes:UP000001052};
RN   [1] {ECO:0000313|Proteomes:UP000001052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5692 {ECO:0000313|Proteomes:UP000001052};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Mikhailova N., Munk A.C., Brettin T., Detter J.C., Han C., Tapia R.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Spring S., Klenk H.-P., Eisen J.A.;
RT   "The complete chromosome of Desulfohalobium retbaense DSM 5692.";
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACV69416.1, ECO:0000313|Proteomes:UP000001052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5692 {ECO:0000313|EMBL:ACV69416.1,
RC   ECO:0000313|Proteomes:UP000001052};
RX   PubMed=21304676;
RA   Spring S., Nolan M., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA   Cheng J.F., Lucas S., Land M., Chen F., Bruce D., Goodwin L., Pitluck S.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Munk C., Kiss H., Chain P., Han C.,
RA   Brettin T., Detter J.C., Schuler E., Goker M., Rohde M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Desulfohalobium retbaense type strain
RT   (HR(100)).";
RL   Stand. Genomic Sci. 2:38-48(2010).
CC   -!- FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA (AcCoA),
CC       an essential intermediate at the junction of anabolic and catabolic
CC       pathways. AcsA undergoes a two-step reaction. In the first half
CC       reaction, AcsA combines acetate with ATP to form acetyl-adenylate
CC       (AcAMP) intermediate. In the second half reaction, it can then transfer
CC       the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the
CC       product AcCoA. {ECO:0000256|HAMAP-Rule:MF_01123}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:456215; EC=6.2.1.1; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01123};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01123};
CC   -!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase
CC       activates the enzyme. {ECO:0000256|HAMAP-Rule:MF_01123}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|HAMAP-Rule:MF_01123}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01123}.
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DR   EMBL; CP001734; ACV69416.1; -; Genomic_DNA.
DR   RefSeq; WP_015752557.1; NC_013223.1.
DR   AlphaFoldDB; C8X4E2; -.
DR   STRING; 485915.Dret_2132; -.
DR   KEGG; drt:Dret_2132; -.
DR   eggNOG; COG0365; Bacteria.
DR   HOGENOM; CLU_000022_3_6_7; -.
DR   OrthoDB; 9801302at2; -.
DR   Proteomes; UP000001052; Chromosome.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion 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   HAMAP; MF_01123; Ac_CoA_synth; 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   Acetylation {ECO:0000256|ARBA:ARBA00022990, ECO:0000256|HAMAP-
KW   Rule:MF_01123};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01123};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01123};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01123};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01123};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01123}; Reference proteome {ECO:0000313|Proteomes:UP000001052}.
FT   DOMAIN          36..92
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          96..481
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          542..620
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         203..206
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         322
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         398..400
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         422..427
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         511
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         526
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         534
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         537
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         548
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         550
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         553
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         595
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   MOD_RES         620
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
SQ   SEQUENCE   661 AA;  73245 MW;  0B1F90A93F31B941 CRC64;
     MGGSDEHIES MMHERRHFPP PRHGSERAHI PGPEAYDDLR DQAARDPEGF WAERAKALLD
     WDSEWDTVLE ADWETPEFKW FAGGKLNACA NCLDRHVASG RGEKTALIWQ GEPEDDVRQF
     TYAELRDEVV KFAKVLKKWG VGKGDRVAVY LPMIPELPIA MLACARIGAV HSVVFAGFSA
     HSLQNRIQDC EAKVLITADA VIRAGKQIPL KTNGDEALEA CPSVEHCIVV NRAGLDVAMH
     EGRDVWWHDA VAGDDGTDCP PESMDAEDLL FILYTSGSTG KPKGVVHTTG GYLTYTAQTT
     QWVFDIQEDD VYWCTADIGW ITGHSYILYG PLALGATTVM FEGVPSYPQP DRFWQVVEKF
     KVTIFYTAPT VIRALMREGP QWTETRDLSS LRLLGSVGEP INPEAWMWYH DHVGKGELPV
     LDTWWQTETG GIMISAVPYA TTLKPGSASQ PLPGIEADIV DRDGEPVGPN RGGHLVVKTP
     WPGMLRNVYG DPARYKSTYF ERFPGMYESG DSARMDEEGY FWIMGRLDDV INVSGHRLGT
     AEIESALVAH EAVAEAAVVG MPHEVKGQAI YAYVTLKSTF QENDELRKVL RQHVRTEIGA
     IATPEIIQFA PGLPKTRSGK IMRRILRKIA ADETNAFGDT STLADPTVIA DLIDGKNLLG
     K
//