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Q8ZKF6

- ACSA_SALTY

UniProt

Q8ZKF6 - ACSA_SALTY

Protein

Acetyl-coenzyme A synthetase

Gene

acs

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    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.1 PublicationUniRule annotation
    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

    Magnesium.

    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 A2 PublicationsUniRule annotation
    Binding sitei335 – 3351Coenzyme A2 PublicationsUniRule annotation
    Binding sitei500 – 5001ATP
    Binding sitei515 – 5151ATP
    Sitei517 – 5171Hinge residue important for conformational flexibility
    Binding sitei523 – 5231Coenzyme A; via carbonyl oxygen2 PublicationsUniRule annotation
    Binding sitei526 – 5261ATP
    Metal bindingi537 – 5371Magnesium; via carbonyl oxygen
    Metal bindingi539 – 5391Magnesium; via carbonyl oxygen
    Metal bindingi542 – 5421Magnesium; via carbonyl oxygen
    Binding sitei584 – 5841Coenzyme A2 PublicationsUniRule annotation

    Regions

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

    GO - Molecular functioni

    1. acetate-CoA ligase activity Source: UniProtKB-HAMAP
    2. AMP binding Source: InterPro
    3. ATP binding Source: UniProtKB-KW
    4. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. acetyl-CoA biosynthetic process from acetate Source: UniProtKB-HAMAP
    2. chemotaxis Source: UniProtKB-HAMAP

    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: 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 Pat2 PublicationsUniRule annotation

    Post-translational modificationi

    Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme.2 PublicationsUniRule annotation

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    OMAiAWIWYRD.
    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

    MSQTHKHAIP ANIADRCLIN PEQYETKYKQ SINDPDTFWG EQGKILDWIT    50
    PYQKVKNTSF APGNVSIKWY EDGTLNLAAN CLDRHLQENG DRTAIIWEGD 100
    DTSQSKHISY RELHRDVCRF ANTLLDLGIK KGDVVAIYMP MVPEAAVAML 150
    ACARIGAVHS VIFGGFSPEA VAGRIIDSSS RLVITADEGV RAGRSIPLKK 200
    NVDDALKNPN VTSVEHVIVL KRTGSDIDWQ EGRDLWWRDL IEKASPEHQP 250
    EAMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAATTFK YVFDYHPGDI 300
    YWCTADVGWV TGHSYLLYGP LACGATTLMF EGVPNWPTPA RMCQVVDKHQ 350
    VNILYTAPTA IRALMAEGDK AIEGTDRSSL RILGSVGEPI NPEAWEWYWK 400
    KIGKEKCPVV DTWWQTETGG FMITPLPGAI ELKAGSATRP FFGVQPALVD 450
    NEGHPQEGAT EGNLVITDSW PGQARTLFGD HERFEQTYFS TFKNMYFSGD 500
    GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVAHP KIAEAAVVGI 550
    PHAIKGQAIY AYVTLNHGEE PSPELYAEVR NWVRKEIGPL ATPDVLHWTD 600
    SLPKTRSGKI MRRILRKIAA GDTSNLGDTS TLADPGVVEK LLEEKQAIAM 650
    PS 652
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE006468 Genomic DNA. Translation: AAL23099.1.
    RefSeqiNP_463140.1. NC_003197.1.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE006468 Genomic DNA. Translation: AAL23099.1 .
    RefSeqi NP_463140.1. NC_003197.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PG3 X-ray 2.30 A/B 1-652 [» ]
    1PG4 X-ray 1.75 A/B 1-652 [» ]
    2P20 X-ray 2.22 A/B 1-652 [» ]
    2P2B X-ray 2.20 A/B 1-652 [» ]
    2P2F X-ray 2.58 A/B 1-652 [» ]
    2P2J X-ray 2.30 A/B 1-652 [» ]
    2P2M X-ray 2.11 A/B 1-652 [» ]
    2P2Q X-ray 2.42 A/B 1-652 [» ]
    ProteinModelPortali Q8ZKF6.
    SMRi Q8ZKF6. Positions 5-647.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 99287.STM4275.

    Proteomic databases

    PaxDbi Q8ZKF6.
    PRIDEi Q8ZKF6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL23099 ; AAL23099 ; STM4275 .
    GeneIDi 1255801.
    KEGGi stm:STM4275.
    PATRICi 32387457. VBISalEnt20916_4496.

    Phylogenomic databases

    eggNOGi COG0365.
    HOGENOMi HOG000229981.
    KOi K01895.
    OMAi AWIWYRD.
    OrthoDBi EOG68WR2H.
    PhylomeDBi Q8ZKF6.

    Enzyme and pathway databases

    BioCyci SENT99287:GCTI-4306-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q8ZKF6.

    Family and domain databases

    HAMAPi MF_01123. Ac_CoA_synth.
    InterProi IPR011904. Ac_CoA_lig.
    IPR025110. AMP-bd_C.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view ]
    Pfami PF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR02188. Ac_CoA_lig_AcsA. 1 hit.
    PROSITEi PS00455. AMP_BINDING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 83 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