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Q8ZKF6

- ACSA_SALTY

UniProt

Q8ZKF6 - ACSA_SALTY

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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

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
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: 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

        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:
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

« 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: 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