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B5R939

- B5R939_SALG2

UniProt

B5R939 - B5R939_SALG2

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Protein
Acetyl-coenzyme A synthetase
Gene
acs, SG4119
Organism
Salmonella gallinarum (strain 287/91 / NCTC 13346)
Status
Unreviewed - 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 By similarity.UniRule annotation
Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA 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 By similarity.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 By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Magnesium By similarity.UniRule annotationSAAS annotations

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei311 – 3111Coenzyme A By similarityUniRule annotation
Binding sitei335 – 3351Coenzyme A By similarityUniRule annotation
Binding sitei387 – 3871Substrate; via nitrogen amide By similarityUniRule annotation
Binding sitei500 – 5001Substrate By similarityUniRule annotation
Binding sitei515 – 5151Substrate By similarityUniRule annotation
Active sitei517 – 5171 By similarityUniRule annotation
Binding sitei523 – 5231Coenzyme A By similarityUniRule annotation
Binding sitei526 – 5261Substrate By similarityUniRule annotation
Metal bindingi537 – 5371Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi539 – 5391Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi542 – 5421Magnesium; via carbonyl oxygen By similarityUniRule annotation
Binding sitei584 – 5841Coenzyme A By similarityUniRule annotation

GO - Molecular functioni

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

LigaseUniRule annotationImported

Keywords - Ligandi

ATP-bindingUniRule annotation, MagnesiumUniRule annotationSAAS annotations, Metal-bindingUniRule annotationSAAS annotations, Nucleotide-binding

Enzyme and pathway databases

BioCyciSENT550538:GJ93-4067-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 ligase
Acyl-activating enzyme
Gene namesi
Name:acsUniRule annotationImported
Ordered Locus Names:SG4119Imported
OrganismiSalmonella gallinarum (strain 287/91 / NCTC 13346)Imported
Taxonomic identifieri550538 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000008321: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei609 – 6091N6-acetyllysine By similarityUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

AcetylationUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi550538.SG4119.

Structurei

3D structure databases

ProteinModelPortaliB5R939.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni191 – 1944Coenzyme A By similarityUniRule annotation
Regioni411 – 4166Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
OMAiAWIWYRD.
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.

B5R939-1 [UniParc]FASTAAdd to Basket

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MSQTHKHAIP ANIADRCLIN PEQYETKYKQ SINDPDTFWG EQGKILDWIT    50
PYQKVKNTSF APGNVSIKWY EDGTLNLAAN CLDRHLQENG DRTAIIWEGD 100
DASQSKHISY RELHRDVCRF ANTLLDLGIK KGDVVAIYMP MVPEAAVAML 150
ACARIGAVHS VIFGGFSPEA VAGRIIDSSS RLVITADEGV RAGRSIPLKK 200
NVDDALKNPN VTSVEHVIVL KRTDSDIDWQ 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):72,181
Last modified:November 4, 2008 - v1
Checksum:i5544EBC7416BEEF5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM933173 Genomic DNA. Translation: CAR39886.1.
RefSeqiYP_002228846.1. NC_011274.1.

Genome annotation databases

EnsemblBacteriaiCAR39886; CAR39886; EBG00000230715.
PATRICi18507047. VBISalEnt1629_4376.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM933173 Genomic DNA. Translation: CAR39886.1 .
RefSeqi YP_002228846.1. NC_011274.1.

3D structure databases

ProteinModelPortali B5R939.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 550538.SG4119.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAR39886 ; CAR39886 ; EBG00000230715 .
PATRICi 18507047. VBISalEnt1629_4376.

Phylogenomic databases

eggNOGi COG0365.
HOGENOMi HOG000229981.
OMAi AWIWYRD.
OrthoDBi EOG68WR2H.

Enzyme and pathway databases

BioCyci SENT550538:GJ93-4067-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: 287/91 / NCTC 13346.

Entry informationi

Entry nameiB5R939_SALG2
AccessioniPrimary (citable) accession number: B5R939
Entry historyi
Integrated into UniProtKB/TrEMBL: November 4, 2008
Last sequence update: November 4, 2008
Last modified: June 11, 2014
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

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