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Protein

Acetyl-coenzyme A synthetase

Gene

acs

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.UniRule annotation1 Publication
Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis.UniRule annotation

Catalytic activityi

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.UniRule annotation

Cofactori

Kineticsi

  1. KM=77.1 µM for ATP (at pH 7.5 and at 37 degrees Celsius)1 Publication
  2. KM=50 µM for CoA (at pH 7.5 and at 37 degrees Celsius)1 Publication
  3. KM=6047 µM for acetate (at pH 7.5 and at 37 degrees Celsius)1 Publication
  4. KM=9413 µM for propionate (at pH 7.5 and at 37 degrees Celsius)1 Publication
  5. KM=9450 µM for glycine (at pH 7.5 and at 37 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei311 – 3111Coenzyme AUniRule annotation2 Publications
    Binding sitei335 – 3351Coenzyme AUniRule annotation2 Publications
    Binding sitei500 – 5001ATP
    Binding sitei515 – 5151ATP
    Sitei517 – 5171Hinge residue important for conformational flexibility
    Binding sitei523 – 5231Coenzyme A; via carbonyl oxygenUniRule annotation2 Publications
    Binding sitei526 – 5261ATP
    Metal bindingi537 – 5371Magnesium; via carbonyl oxygen
    Metal bindingi539 – 5391Magnesium; via carbonyl oxygen
    Metal bindingi542 – 5421Magnesium; via carbonyl oxygen
    Binding sitei584 – 5841Coenzyme AUniRule annotation2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi387 – 3893ATP
    Nucleotide bindingi411 – 4166ATP

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Ligase

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciSENT99287:GCTI-4306-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyl-coenzyme A synthetaseUniRule annotation (EC:6.2.1.1UniRule annotation)
    Short name:
    AcCoA synthetaseUniRule annotation
    Short name:
    AcsUniRule annotation
    Alternative name(s):
    Acetate--CoA ligaseUniRule annotation
    Acyl-activating enzymeUniRule annotation
    Gene namesi
    Name:acsUniRule annotation
    Ordered Locus Names:STM4275
    OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
    Taxonomic identifieri99287 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
    ProteomesiUP000001014 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi194 – 1941R → A: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 2-fold increase in the affinity for ATP and 3-fold reduction for CoA. 1 Publication
    Mutagenesisi194 – 1941R → E: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 2-fold increase in the affinity for ATP and 2-fold reduction for CoA. 1 Publication
    Mutagenesisi357 – 3571A → V: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 3-fold increase in the affinity for ATP and 3-fold reduction for CoA. 1 Publication
    Mutagenesisi517 – 5171D → G: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 2-fold increase in the affinity for ATP and 10-fold reduction for CoA. 1 Publication
    Mutagenesisi517 – 5171D → P: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 3-fold reduction in the affinity for ATP and 4.5-fold reduction for CoA. 1 Publication
    Mutagenesisi524 – 5241G → L: No acetyl-coenzyme A synthetase activity. 1 Publication
    Mutagenesisi524 – 5241G → S: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. Almost the same affinity as the wild-type for ATP, but 9-fold reduction in the affinity for CoA. 1 Publication
    Mutagenesisi526 – 5261R → A: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 3-fold increase in the affinity for ATP and 4-fold reduction for CoA. 1 Publication
    Mutagenesisi584 – 5841R → A: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 2-fold increase in the affinity for ATP and 7-fold reduction for CoA. 1 Publication
    Mutagenesisi584 – 5841R → E: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 3-fold increase in the affinity for ATP and 8-fold reduction for CoA. 1 Publication
    Mutagenesisi609 – 6091K → A: No acetyl-coenzyme A synthetase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 652652Acetyl-coenzyme A synthetasePRO_0000208386Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei609 – 6091N6-acetyllysine; by PatUniRule annotation2 Publications

    Post-translational modificationi

    Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme.UniRule annotation2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ8ZKF6.
    PRIDEiQ8ZKF6.

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Protein-protein interaction databases

    STRINGi99287.STM4275.

    Structurei

    Secondary structure

    1
    652
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi11 – 166Combined sources
    Helixi21 – 3313Combined sources
    Helixi35 – 428Combined sources
    Helixi43 – 453Combined sources
    Beta strandi56 – 594Combined sources
    Beta strandi66 – 705Combined sources
    Helixi77 – 815Combined sources
    Helixi83 – 853Combined sources
    Helixi86 – 894Combined sources
    Beta strandi92 – 987Combined sources
    Beta strandi105 – 1095Combined sources
    Helixi110 – 12718Combined sources
    Beta strandi134 – 1385Combined sources
    Helixi143 – 15513Combined sources
    Beta strandi158 – 1614Combined sources
    Helixi168 – 17811Combined sources
    Beta strandi181 – 19111Combined sources
    Beta strandi194 – 1985Combined sources
    Helixi199 – 2068Combined sources
    Beta strandi216 – 2205Combined sources
    Turni231 – 2333Combined sources
    Beta strandi234 – 2363Combined sources
    Helixi237 – 2415Combined sources
    Beta strandi257 – 2648Combined sources
    Beta strandi267 – 2704Combined sources
    Beta strandi272 – 2787Combined sources
    Helixi279 – 29214Combined sources
    Beta strandi300 – 3034Combined sources
    Helixi310 – 3156Combined sources
    Helixi318 – 3225Combined sources
    Beta strandi326 – 3305Combined sources
    Beta strandi336 – 3383Combined sources
    Helixi341 – 3499Combined sources
    Beta strandi352 – 3565Combined sources
    Helixi358 – 3658Combined sources
    Helixi366 – 3716Combined sources
    Turni372 – 3743Combined sources
    Beta strandi382 – 3887Combined sources
    Helixi392 – 40110Combined sources
    Turni402 – 4054Combined sources
    Beta strandi409 – 4135Combined sources
    Helixi416 – 4183Combined sources
    Turni427 – 4293Combined sources
    Beta strandi438 – 4403Combined sources
    Beta strandi446 – 4494Combined sources
    Beta strandi458 – 4669Combined sources
    Helixi481 – 4899Combined sources
    Beta strandi490 – 4923Combined sources
    Beta strandi495 – 50410Combined sources
    Beta strandi510 – 52213Combined sources
    Beta strandi525 – 5284Combined sources
    Helixi529 – 53810Combined sources
    Beta strandi542 – 55211Combined sources
    Turni553 – 5553Combined sources
    Beta strandi556 – 56510Combined sources
    Helixi573 – 58614Combined sources
    Helixi589 – 5913Combined sources
    Beta strandi594 – 5985Combined sources
    Beta strandi604 – 6074Combined sources
    Helixi612 – 6209Combined sources
    Helixi629 – 6313Combined sources
    Beta strandi632 – 6343Combined sources
    Helixi637 – 64610Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PG3X-ray2.30A/B1-652[»]
    1PG4X-ray1.75A/B1-652[»]
    2P20X-ray2.22A/B1-652[»]
    2P2BX-ray2.20A/B1-652[»]
    2P2FX-ray2.58A/B1-652[»]
    2P2JX-ray2.30A/B1-652[»]
    2P2MX-ray2.11A/B1-652[»]
    2P2QX-ray2.42A/B1-652[»]
    ProteinModelPortaliQ8ZKF6.
    SMRiQ8ZKF6. Positions 5-647.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8ZKF6.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni191 – 1944Coenzyme A binding

    Sequence similaritiesi

    Belongs to the ATP-dependent AMP-binding enzyme family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0365.
    HOGENOMiHOG000229981.
    KOiK01895.
    OMAiSHRCLTI.
    OrthoDBiEOG68WR2H.
    PhylomeDBiQ8ZKF6.

    Family and domain databases

    HAMAPiMF_01123. Ac_CoA_synth.
    InterProiIPR011904. Ac_CoA_lig.
    IPR025110. AMP-bd_C.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view]
    PfamiPF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
    PROSITEiPS00455. AMP_BINDING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8ZKF6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSQTHKHAIP ANIADRCLIN PEQYETKYKQ SINDPDTFWG EQGKILDWIT
    60 70 80 90 100
    PYQKVKNTSF APGNVSIKWY EDGTLNLAAN CLDRHLQENG DRTAIIWEGD
    110 120 130 140 150
    DTSQSKHISY RELHRDVCRF ANTLLDLGIK KGDVVAIYMP MVPEAAVAML
    160 170 180 190 200
    ACARIGAVHS VIFGGFSPEA VAGRIIDSSS RLVITADEGV RAGRSIPLKK
    210 220 230 240 250
    NVDDALKNPN VTSVEHVIVL KRTGSDIDWQ EGRDLWWRDL IEKASPEHQP
    260 270 280 290 300
    EAMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAATTFK YVFDYHPGDI
    310 320 330 340 350
    YWCTADVGWV TGHSYLLYGP LACGATTLMF EGVPNWPTPA RMCQVVDKHQ
    360 370 380 390 400
    VNILYTAPTA IRALMAEGDK AIEGTDRSSL RILGSVGEPI NPEAWEWYWK
    410 420 430 440 450
    KIGKEKCPVV DTWWQTETGG FMITPLPGAI ELKAGSATRP FFGVQPALVD
    460 470 480 490 500
    NEGHPQEGAT EGNLVITDSW PGQARTLFGD HERFEQTYFS TFKNMYFSGD
    510 520 530 540 550
    GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVAHP KIAEAAVVGI
    560 570 580 590 600
    PHAIKGQAIY AYVTLNHGEE PSPELYAEVR NWVRKEIGPL ATPDVLHWTD
    610 620 630 640 650
    SLPKTRSGKI MRRILRKIAA GDTSNLGDTS TLADPGVVEK LLEEKQAIAM

    PS
    Length:652
    Mass (Da):72,153
    Last modified:March 1, 2002 - v1
    Checksum:i347209D1D3D349D8
    GO

    Mass spectrometryi

    Molecular mass is 733.4 Da from positions 607 - 612. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE006468 Genomic DNA. Translation: AAL23099.1.
    RefSeqiNP_463140.1. NC_003197.1.
    WP_000083882.1. NC_003197.1.

    Genome annotation databases

    EnsemblBacteriaiAAL23099; AAL23099; STM4275.
    GeneIDi1255801.
    KEGGistm:STM4275.
    PATRICi32387457. VBISalEnt20916_4496.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE006468 Genomic DNA. Translation: AAL23099.1.
    RefSeqiNP_463140.1. NC_003197.1.
    WP_000083882.1. NC_003197.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PG3X-ray2.30A/B1-652[»]
    1PG4X-ray1.75A/B1-652[»]
    2P20X-ray2.22A/B1-652[»]
    2P2BX-ray2.20A/B1-652[»]
    2P2FX-ray2.58A/B1-652[»]
    2P2JX-ray2.30A/B1-652[»]
    2P2MX-ray2.11A/B1-652[»]
    2P2QX-ray2.42A/B1-652[»]
    ProteinModelPortaliQ8ZKF6.
    SMRiQ8ZKF6. Positions 5-647.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi99287.STM4275.

    Proteomic databases

    PaxDbiQ8ZKF6.
    PRIDEiQ8ZKF6.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAL23099; AAL23099; STM4275.
    GeneIDi1255801.
    KEGGistm:STM4275.
    PATRICi32387457. VBISalEnt20916_4496.

    Phylogenomic databases

    eggNOGiCOG0365.
    HOGENOMiHOG000229981.
    KOiK01895.
    OMAiSHRCLTI.
    OrthoDBiEOG68WR2H.
    PhylomeDBiQ8ZKF6.

    Enzyme and pathway databases

    BioCyciSENT99287:GCTI-4306-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiQ8ZKF6.

    Family and domain databases

    HAMAPiMF_01123. Ac_CoA_synth.
    InterProiIPR011904. Ac_CoA_lig.
    IPR025110. AMP-bd_C.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view]
    PfamiPF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
    PROSITEiPS00455. AMP_BINDING. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: LT2 / SGSC1412 / ATCC 700720.
    2. "Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine."
      Starai V.J., Celic I., Cole R.N., Boeke J.D., Escalante-Semerena J.C.
      Science 298:2390-2392(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-609, DEACETYLATION BY SIR2 HOMOLOG, MASS SPECTROMETRY.
      Strain: LT2 / SGSC1412 / ATCC 700720.
    3. "Identification of the protein acetyltransferase (Pat) enzyme that acetylates acetyl-CoA synthetase in Salmonella enterica."
      Starai V.J., Escalante-Semerena J.C.
      J. Mol. Biol. 340:1005-1012(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-609.
      Strain: LT2.
    4. "The 1.75 A crystal structure of acetyl-CoA synthetase bound to adenosine-5'-propylphosphate and coenzyme A."
      Gulick A.M., Starai V.J., Horswill A.R., Homick K.M., Escalante-Semerena J.C.
      Biochemistry 42:2866-2873(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH ATP ANALOG AND COENZYME A, SUBUNIT.
    5. "Biochemical and crystallographic analysis of substrate binding and conformational changes in acetyl-CoA synthetase."
      Reger A.S., Carney J.M., Gulick A.M.
      Biochemistry 46:6536-6546(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF WILD-TYPE AND MUTANTS IN COMPLEX WITH THE ATP ANALOG AMP; COENZYME A AND MAGNESIUM IONS, FUNCTION, MUTAGENESIS OF ARG-194; ALA-357; ASP-517; GLY-524; ARG-526; ARG-584 AND LYS-609, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

    Entry informationi

    Entry nameiACSA_SALTY
    AccessioniPrimary (citable) accession number: Q8ZKF6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2003
    Last sequence update: March 1, 2002
    Last modified: June 24, 2015
    This is version 87 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.