AACS_RHIME
ID AACS_RHIME Reviewed; 650 AA.
AC Q9Z3R3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Acetoacetyl-coenzyme A synthetase {ECO:0000303|PubMed:10735852};
DE Short=Acetoacetyl-CoA synthetase {ECO:0000303|PubMed:10735852};
DE EC=6.2.1.16 {ECO:0000305|PubMed:10735852};
GN Name=acsA2 {ECO:0000312|EMBL:CAC45291.1};
GN Synonyms=acsA {ECO:0000303|PubMed:10735852}; OrderedLocusNames=R00719;
GN ORFNames=SMc00774;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP PATHWAY.
RC STRAIN=SU47 / 1021;
RX PubMed=10735852; DOI=10.1128/jb.182.8.2113-2118.2000;
RA Cai G.-Q., Driscoll B.T., Charles T.C.;
RT "Requirement for the enzymes acetoacetyl coenzyme A synthetase and poly-3-
RT hydroxybutyrate (PHB) synthase for growth of Sinorhizobium meliloti on PHB
RT cycle intermediates.";
RL J. Bacteriol. 182:2113-2118(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
CC -!- FUNCTION: Catalyzes the conversion of acetoacetate into acetoacetyl-
CC CoA. Is involved in poly-3-hydroxybutyrate (PHB) degradation, which
CC allows growth of R.meliloti on PHB cycle intermediates.
CC {ECO:0000269|PubMed:10735852}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetoacetate + ATP + CoA = acetoacetyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:16117, ChEBI:CHEBI:13705,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57286,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:456215; EC=6.2.1.16;
CC Evidence={ECO:0000305|PubMed:10735852};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8ZKF6};
CC -!- PATHWAY: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate
CC degradation. {ECO:0000269|PubMed:10735852}.
CC -!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase
CC activates the enzyme. {ECO:0000250|UniProtKB:Q8ZKF6}.
CC -!- DISRUPTION PHENOTYPE: Acetyl-CoA synthetase activity is not affected in
CC mutant cells, whereas acetoacetyl-CoA synthetase activity is
CC drastically reduced. Moreover, after growth in YM medium, cells lacking
CC this gene accumulate PHB to 60 to 70% of cell dry mass. They display
CC reduced ability to proliferate during the first 30 days of incubation
CC in growth medium lacking nutrient carbon.
CC {ECO:0000269|PubMed:10735852}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AF080217; AAC64548.1; -; Genomic_DNA.
DR EMBL; AL591688; CAC45291.1; -; Genomic_DNA.
DR RefSeq; NP_384825.1; NC_003047.1.
DR RefSeq; WP_010968769.1; NC_003047.1.
DR AlphaFoldDB; Q9Z3R3; -.
DR SMR; Q9Z3R3; -.
DR STRING; 266834.SMc00774; -.
DR EnsemblBacteria; CAC45291; CAC45291; SMc00774.
DR GeneID; 61602185; -.
DR KEGG; sme:SMc00774; -.
DR PATRIC; fig|266834.11.peg.2098; -.
DR eggNOG; COG0365; Bacteria.
DR HOGENOM; CLU_000022_3_3_5; -.
DR OMA; WYSSTGW; -.
DR BRENDA; 6.2.1.16; 5347.
DR UniPathway; UPA01062; -.
DR Proteomes; UP000001976; Chromosome.
DR GO; GO:0030729; F:acetoacetate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR005914; Acac_CoA_synth.
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.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR TIGRFAMs; TIGR01217; ac_ac_CoA_syn; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW Acetylation; ATP-binding; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..650
FT /note="Acetoacetyl-coenzyme A synthetase"
FT /id="PRO_0000208381"
FT BINDING 199..202
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6"
FT BINDING 392..394
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6"
FT BINDING 504
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6"
FT BINDING 519
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6"
FT BINDING 530
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6"
FT BINDING 546
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6"
FT BINDING 587
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6"
FT MOD_RES 612
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6"
FT CONFLICT 144
FT /note="A -> S (in Ref. 1; AAC64548)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="G -> C (in Ref. 1; AAC64548)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="V -> L (in Ref. 1; AAC64548)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="L -> V (in Ref. 1; AAC64548)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 650 AA; 71309 MW; AE2B7A41E6C57846 CRC64;
MQAERPLWVP DREIVERSPM AEFIDWCGER FGRSFADYDA FHDWSVSERG AFWTAVWEHC
KVIGESGEKA LVDGDRMLDA RFFPEARLNF AENLLRKTGS GDALIFRGED KVSYRLTWDE
LRALVSRLQQ ALRAQGIGAG DRVAAMMPNM PETIALMLAT ASVGAIWSSC SPDFGEQGVL
DRFGQIAPKL FIVCDGYWYN GKRQDVDSKV RAVAKSLGAP TVIVPYAGDS AALAPTVEGG
VTLADFIAGF QAGPLVFERL PFGHPLYILF SSGTTGVPKC IVHSAGGTLL QHLKEHRFHC
GLRDGERLFY FTTCGWMMWN WLASGLAVGA TLCLYDGSPF CPDGNVLFDY AAAERFAVFG
TSAKYIDAVR KGGFTPARTH DLSSLRLMTS TGSPLSPEGF SFVYEGIKPD VQLASISGGT
DIVSCFVLGN PLKPVWRGEI QGPGLGLAVD VWNDEGKPVR GEKGELVCTR AFPSMPVMFW
NDPDGAKYRA AYFDRFDNVW CHGDFAEWTP HGGIVIHGRS DATLNPGGVR IGTAEIYNQV
EQMDEVAEAL CIGQDWEDDV RVVLFVRLAR GVELTEALTR EIKNRIRSGA SPRHVPAKII
AVADIPRTKS GKIVELAVRD VVHGRPVKNK EALANPEALD LFAGLEELKS
