ACSA2_PSEPK
ID ACSA2_PSEPK Reviewed; 644 AA.
AC Q88DW6;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Acetyl-coenzyme A synthetase 2 {ECO:0000255|HAMAP-Rule:MF_01123};
DE Short=AcCoA synthetase 2 {ECO:0000255|HAMAP-Rule:MF_01123};
DE Short=Acs 2 {ECO:0000255|HAMAP-Rule:MF_01123};
DE EC=6.2.1.1 {ECO:0000255|HAMAP-Rule:MF_01123};
DE AltName: Full=Acetate--CoA ligase 2 {ECO:0000255|HAMAP-Rule:MF_01123};
DE AltName: Full=Acyl-activating enzyme 2 {ECO:0000255|HAMAP-Rule:MF_01123};
GN Name=acsA2 {ECO:0000255|HAMAP-Rule:MF_01123}; Synonyms=acsB;
GN OrderedLocusNames=PP_4702;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
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:0000255|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:0000255|HAMAP-
CC Rule:MF_01123};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01123};
CC -!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase
CC activates the enzyme. {ECO:0000255|HAMAP-Rule:MF_01123}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000255|HAMAP-Rule:MF_01123}.
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DR EMBL; AE015451; AAN70275.1; -; Genomic_DNA.
DR RefSeq; NP_746811.1; NC_002947.4.
DR RefSeq; WP_010955351.1; NC_002947.4.
DR AlphaFoldDB; Q88DW6; -.
DR SMR; Q88DW6; -.
DR STRING; 160488.PP_4702; -.
DR PRIDE; Q88DW6; -.
DR EnsemblBacteria; AAN70275; AAN70275; PP_4702.
DR KEGG; ppu:PP_4702; -.
DR PATRIC; fig|160488.4.peg.5012; -.
DR eggNOG; COG0365; Bacteria.
DR HOGENOM; CLU_000022_3_6_6; -.
DR OMA; AIKASWP; -.
DR PhylomeDB; Q88DW6; -.
DR BioCyc; PPUT160488:G1G01-5023-MON; -.
DR Proteomes; UP000000556; 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 Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 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.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR TIGRFAMs; TIGR02188; Ac_CoA_lig_AcsA; 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..644
FT /note="Acetyl-coenzyme A synthetase 2"
FT /id="PRO_0000208377"
FT BINDING 189..192
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 307
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 331
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 383..385
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 407..412
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 496
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 511
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 519
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 522
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 533
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 535
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 538
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT MOD_RES 605
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
SQ SEQUENCE 644 AA; 71251 MW; 82D98FD672B86A9A CRC64;
MFDIRKYPQA LAVSQSAALT PEDYRRLYRQ SVEDPDTFWA EQAKRLDWIK PWSSVQQCDL
HTGKARWFDG AQLNVSYNCI DRHLAQRGEQ TALLWEGDDP KDSKAITYRE LHRQVCRLAN
AMKARGVKKG DRVSIYMPMI PEAAFAMLAC TRIGAIHSVV FGGFSPDALR DRILDADCRT
VITADEGVRG GKRIPLKQNV DKALASCPAV SSVLVVRRTG GDVAWTEGRD LWYHEATKDA
GDDCPPEPME AEDPLFILYT SGSTGKPKGV LHTTGGYLLQ ATMTFKVVFD YRDGEVFWCT
ADVGWVTGHS YIVYGPLANG AISLMFEGVP NYPDTSRFWQ VVDKHQVNIF YTAPTALRAL
MREGSAPLQS TSRKSLRLLG SVGEPINPEA WEWYFEEVGQ KRCPIVDTWW QTETGGIMLT
PLPGTQSLKP GCATQPMFGV QPVLLDEKGK LIEGPGAGVL AIKASWPGQI RSVYGDHQRM
VDTYFKPLPG YYFTGDGARR DADGDYWITG RIDDVINVSG HRIGTAEVES ALVLHDSVAE
AAVVGYPHDL KGQGVYAFVT TMNGVTPDDT LKAELLALVS KEIGSFAKPE LIQWAPALPK
TRSGKIMRRI LRKIACNELE NLGDTSTLAD PSVVQGLIDK RLNQ
