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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)DescriptionActionsGraphical viewLength
    Binding sitei311Coenzyme AUniRule annotation2 Publications1
    Binding sitei335Coenzyme AUniRule annotation2 Publications1
    Binding sitei500ATP1
    Binding sitei515ATP1
    Sitei517Hinge residue important for conformational flexibility1
    Binding sitei523Coenzyme A; via carbonyl oxygenUniRule annotation2 Publications1
    Binding sitei526ATP1
    Metal bindingi537Magnesium; via carbonyl oxygen1
    Metal bindingi539Magnesium; via carbonyl oxygen1
    Metal bindingi542Magnesium; via carbonyl oxygen1
    Binding sitei584Coenzyme AUniRule annotation2 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi387 – 389ATP3
    Nucleotide bindingi411 – 416ATP6

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Ligase

    Keywords - Ligandi

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

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
    Proteomesi
    • UP000001014 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi194R → 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 Publication1
    Mutagenesisi194R → 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 Publication1
    Mutagenesisi357A → 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 Publication1
    Mutagenesisi517D → 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 Publication1
    Mutagenesisi517D → 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 Publication1
    Mutagenesisi524G → L: No acetyl-coenzyme A synthetase activity. 1 Publication1
    Mutagenesisi524G → 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 Publication1
    Mutagenesisi526R → 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 Publication1
    Mutagenesisi584R → 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 Publication1
    Mutagenesisi584R → 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 Publication1
    Mutagenesisi609K → A: No acetyl-coenzyme A synthetase activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002083861 – 652Acetyl-coenzyme A synthetaseAdd BLAST652

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei609N6-acetyllysine; by PatUniRule annotation2 Publications1

    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

    1652
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi11 – 16Combined sources6
    Helixi21 – 33Combined sources13
    Helixi35 – 42Combined sources8
    Helixi43 – 45Combined sources3
    Beta strandi56 – 59Combined sources4
    Beta strandi66 – 70Combined sources5
    Helixi77 – 81Combined sources5
    Helixi83 – 85Combined sources3
    Helixi86 – 89Combined sources4
    Beta strandi92 – 98Combined sources7
    Beta strandi105 – 109Combined sources5
    Helixi110 – 127Combined sources18
    Beta strandi134 – 138Combined sources5
    Helixi143 – 155Combined sources13
    Beta strandi158 – 161Combined sources4
    Helixi168 – 178Combined sources11
    Beta strandi181 – 191Combined sources11
    Beta strandi194 – 198Combined sources5
    Helixi199 – 206Combined sources8
    Beta strandi216 – 220Combined sources5
    Turni231 – 233Combined sources3
    Beta strandi234 – 236Combined sources3
    Helixi237 – 241Combined sources5
    Beta strandi257 – 264Combined sources8
    Beta strandi267 – 270Combined sources4
    Beta strandi272 – 278Combined sources7
    Helixi279 – 292Combined sources14
    Beta strandi300 – 303Combined sources4
    Helixi310 – 315Combined sources6
    Helixi318 – 322Combined sources5
    Beta strandi326 – 330Combined sources5
    Beta strandi336 – 338Combined sources3
    Helixi341 – 349Combined sources9
    Beta strandi352 – 356Combined sources5
    Helixi358 – 365Combined sources8
    Helixi366 – 371Combined sources6
    Turni372 – 374Combined sources3
    Beta strandi382 – 388Combined sources7
    Helixi392 – 401Combined sources10
    Turni402 – 405Combined sources4
    Beta strandi409 – 413Combined sources5
    Helixi416 – 418Combined sources3
    Turni427 – 429Combined sources3
    Beta strandi438 – 440Combined sources3
    Beta strandi446 – 449Combined sources4
    Beta strandi458 – 466Combined sources9
    Helixi481 – 489Combined sources9
    Beta strandi490 – 492Combined sources3
    Beta strandi495 – 504Combined sources10
    Beta strandi510 – 522Combined sources13
    Beta strandi525 – 528Combined sources4
    Helixi529 – 538Combined sources10
    Beta strandi542 – 552Combined sources11
    Turni553 – 555Combined sources3
    Beta strandi556 – 565Combined sources10
    Helixi573 – 586Combined sources14
    Helixi589 – 591Combined sources3
    Beta strandi594 – 598Combined sources5
    Beta strandi604 – 607Combined sources4
    Helixi612 – 620Combined sources9
    Helixi629 – 631Combined sources3
    Beta strandi632 – 634Combined sources3
    Helixi637 – 646Combined sources10

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8ZKF6.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni191 – 194Coenzyme A binding4

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiENOG4108IQF. Bacteria.
    COG0365. LUCA.
    HOGENOMiHOG000229981.
    KOiK01895.
    OMAiEGAPNWP.
    PhylomeDBiQ8ZKF6.

    Family and domain databases

    CDDicd05966. ACS. 1 hit.
    HAMAPiMF_01123. Ac_CoA_synth. 1 hit.
    InterProiIPR011904. Ac_CoA_lig.
    IPR032387. ACAS_N.
    IPR025110. AMP-bd_C.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view]
    PfamiPF16177. ACAS_N. 1 hit.
    PF00501. 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
    PDB 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.
    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

    eggNOGiENOG4108IQF. Bacteria.
    COG0365. LUCA.
    HOGENOMiHOG000229981.
    KOiK01895.
    OMAiEGAPNWP.
    PhylomeDBiQ8ZKF6.

    Miscellaneous databases

    EvolutionaryTraceiQ8ZKF6.

    Family and domain databases

    CDDicd05966. ACS. 1 hit.
    HAMAPiMF_01123. Ac_CoA_synth. 1 hit.
    InterProiIPR011904. Ac_CoA_lig.
    IPR032387. ACAS_N.
    IPR025110. AMP-bd_C.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view]
    PfamiPF16177. ACAS_N. 1 hit.
    PF00501. 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...

    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: November 2, 2016
    This is version 94 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

    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 one 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.