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A4TS06

- ACSA_YERPP

UniProt

A4TS06 - ACSA_YERPP

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Protein

Acetyl-coenzyme A synthetase

Gene

acs

Organism
Yersinia pestis (strain Pestoides F)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

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 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

Mg2+UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei311 – 3111Coenzyme AUniRule annotation
Binding sitei335 – 3351Coenzyme AUniRule annotation
Binding sitei500 – 5001ATPUniRule annotation
Binding sitei515 – 5151ATPUniRule annotation
Binding sitei523 – 5231Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei526 – 5261ATPUniRule annotation
Metal bindingi537 – 5371Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi539 – 5391Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi542 – 5421Magnesium; via carbonyl oxygenUniRule annotation
Binding sitei584 – 5841Coenzyme AUniRule annotation

Regions

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

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

BioCyciYPES386656:GKD7-3806-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:YPDSF_3718
OrganismiYersinia pestis (strain Pestoides F)
Taxonomic identifieri386656 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
ProteomesiUP000000236: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 652652Acetyl-coenzyme A synthetasePRO_1000065336Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei609 – 6091N6-acetyllysineUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiA4TS06.

Interactioni

Protein-protein interaction databases

STRINGi386656.YPDSF_3718.

Structurei

3D structure databases

ProteinModelPortaliA4TS06.
SMRiA4TS06. Positions 5-647.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiKMEHLRI.
OrthoDBiEOG68WR2H.

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.

A4TS06-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSQIHKHPIP AAIAEHALIT PEKYQHYYQQ SVQNPDEFWG EQGKIIDWIK
60 70 80 90 100
PYKTVKNTSF DPGHVSIRWF EDGTLNLAAN CLDRHLAERG DQTAIIWEGD
110 120 130 140 150
DPNQSKTVTY KQLHHDVCQF ANVLKSLGVK KGDVVAIYMP MVPEAAVAML
160 170 180 190 200
ACARIGAVHS VIFGGFSPDA VAGRIIDSHS KLVITADEGI RAGRAIPLKK
210 220 230 240 250
NVDEALKNPA ITSIKNVVVF QRTGNASYWE DGRDVWWHDL IKEASADCPP
260 270 280 290 300
EEMNAEDPLF ILYTSGSTGK PKGVVHTTGG YLVYAALTFK YVFDYHPGDI
310 320 330 340 350
YWCTADVGWV TGHSYLLYGP LACGAITLMF EGVPNYPGVN RLSQVVDKHK
360 370 380 390 400
VNILYTAPTA IRALMAEGDK AIEGTKRDSL RIMGSVGEPI NPEAWEWYYN
410 420 430 440 450
KIGNSKCPIV DTWWQTETGG FMITPLPGAT ELKAGSATRP FFGVQPALVD
460 470 480 490 500
NLGNPQEGVA EGNLVITDSW PGQARTLFGD HERFEQTYFS TFKGMYFSGD
510 520 530 540 550
GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVAHP KIAEAAVVGV
560 570 580 590 600
PHNIKGQAIY AYITLNHGEE PTPELYTEVR NWVRKEIGPL ATPDILHWTD
610 620 630 640 650
SLPKTRSGKI MRRILRKIAT GDTSNLGDTS TLADPSVVEK LLEEKQSMQT

PS
Length:652
Mass (Da):72,072
Last modified:May 15, 2007 - v1
Checksum:i933CF5A79F7E4D63
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000668 Genomic DNA. Translation: ABP42068.1.
RefSeqiYP_001165041.1. NC_009381.1.

Genome annotation databases

EnsemblBacteriaiABP42068; ABP42068; YPDSF_3718.
GeneIDi5063053.
KEGGiypp:YPDSF_3718.
PATRICi18617513. VBIYerPes122972_4612.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000668 Genomic DNA. Translation: ABP42068.1 .
RefSeqi YP_001165041.1. NC_009381.1.

3D structure databases

ProteinModelPortali A4TS06.
SMRi A4TS06. Positions 5-647.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 386656.YPDSF_3718.

Proteomic databases

PRIDEi A4TS06.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABP42068 ; ABP42068 ; YPDSF_3718 .
GeneIDi 5063053.
KEGGi ypp:YPDSF_3718.
PATRICi 18617513. VBIYerPes122972_4612.

Phylogenomic databases

eggNOGi COG0365.
HOGENOMi HOG000229981.
KOi K01895.
OMAi KMEHLRI.
OrthoDBi EOG68WR2H.

Enzyme and pathway databases

BioCyci YPES386656:GKD7-3806-MONOMER.

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: Pestoides F.

Entry informationi

Entry nameiACSA_YERPP
AccessioniPrimary (citable) accession number: A4TS06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 15, 2007
Last modified: November 26, 2014
This is version 50 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

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3