Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

I2EEB1

- I2EEB1_CROSK

UniProt

I2EEB1 - I2EEB1_CROSK

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Acetyl-coenzyme A synthetase

Gene

acs

Organism
Cronobacter sakazakii ES15
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.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

Magnesium.UniRule annotationSAAS 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

LigaseUniRule annotation

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciCSAK1138308:GLC5-451-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 annotationImported
ORF Names:ES15_0440Imported
OrganismiCronobacter sakazakii ES15Imported
Taxonomic identifieri1138308 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCronobacter
ProteomesiUP000002877: Chromosome

PTM / Processingi

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

AcetylationUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliI2EEB1.
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

KOiK01895.

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.

I2EEB1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSQIHKHPIP AAIAERCLIT PEQYDAKYQQ SVHDPDAFWG EQGKILDWIT
60 70 80 90 100
PYQTVKNTSF APGNISIKWY EDGTLNLAAN CLDRHLSERG DQTAIIWEGD
110 120 130 140 150
DATQSKHISY RELHRDVCRF ANTLTSLGIK KGDVVAIYMP MVPEAAVAML
160 170 180 190 200
ACARIGAVHS VIFGGFSPEA VAGRIIDSSA RLVITADEGV RAGRAIPLKK
210 220 230 240 250
NVDDALKNPG VTSVEHVVVL KRTGGNIEWH EGRDLWWSEL VEKASAHHQP
260 270 280 290 300
VEMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAATTFL YAFDYHPGDI
310 320 330 340 350
YWCTADVGWV TGHSYLLYGP LACGATTLMF EGVPNWPSAN RMAQVVDKHK
360 370 380 390 400
VNILYTAPTA IRALMAEGDK AIDGTDRSSL RILGSVGEPI NPEAWEWYWK
410 420 430 440 450
KIGNEKCPVI DTWWQTETGG FMITPLPGAT ELKAGSATRP FFGVQPALVD
460 470 480 490 500
NEGNPQQGAT EGNLVITDSW PGQARTLFGD HERFEQTYFS TFKNMYFSGD
510 520 530 540 550
GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVSHP KIAEAAVVGI
560 570 580 590 600
PHSIKGQAIY AYVTLNHGEE PSAELYSEVR NWVRKEIGPL ATPDVLHWTD
610 620 630 640 650
SLPKTRSGKI MRRILRKIAA GDTSNLGDTS TLADPGVVEK LLEEKQSIAM

PS
Length:652
Mass (Da):71,733
Last modified:July 11, 2012 - v1
Checksum:iD14199F1015FBDFD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003312 Genomic DNA. Translation: AFJ98013.1.
RefSeqiWP_014727971.1. NC_017933.1.
YP_006341524.1. NC_017933.1.

Genome annotation databases

EnsemblBacteriaiAFJ98013; AFJ98013; ES15_0440.
GeneIDi13032260.
KEGGicsk:ES15_0440.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003312 Genomic DNA. Translation: AFJ98013.1 .
RefSeqi WP_014727971.1. NC_017933.1.
YP_006341524.1. NC_017933.1.

3D structure databases

ProteinModelPortali I2EEB1.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AFJ98013 ; AFJ98013 ; ES15_0440 .
GeneIDi 13032260.
KEGGi csk:ES15_0440.

Phylogenomic databases

KOi K01895.

Enzyme and pathway databases

BioCyci CSAK1138308:GLC5-451-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. "Complete Genome Sequence of the Opportunistic Food-Borne Pathogen Cronobacter sakazakii ES15."
    Shin H., Lee J.H., Choi Y., Ryu S.
    J. Bacteriol. 194:4438-4439(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ES15Imported.

Entry informationi

Entry nameiI2EEB1_CROSK
AccessioniPrimary (citable) accession number: I2EEB1
Entry historyi
Integrated into UniProtKB/TrEMBL: July 11, 2012
Last sequence update: July 11, 2012
Last modified: October 29, 2014
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3