SubmitCancel

Skip Header

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

I4ERQ3

- I4ERQ3_MODMB

UniProt

I4ERQ3 - I4ERQ3_MODMB

(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
acsA, MODMU_0609
Organism
Modestobacter marinus (strain BC501)
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. 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

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 sitei313 – 3131Coenzyme A By similarityUniRule annotation
Binding sitei389 – 3891Substrate; via nitrogen amide By similarityUniRule annotation
Binding sitei503 – 5031Substrate By similarityUniRule annotation
Binding sitei518 – 5181Substrate By similarityUniRule annotation
Active sitei520 – 5201 By similarityUniRule annotation
Binding sitei526 – 5261Coenzyme A By similarityUniRule annotation
Binding sitei529 – 5291Substrate By similarityUniRule annotation
Metal bindingi540 – 5401Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi542 – 5421Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi545 – 5451Magnesium; via carbonyl oxygen By similarityUniRule annotation
Binding sitei588 – 5881Coenzyme A By similarityUniRule 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: InterPro
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

BioCyciMMAR477641:GLGK-607-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:acsAUniRule annotationImported
Ordered Locus Names:MODMU_0609Imported
OrganismiModestobacter marinus (strain BC501)
Taxonomic identifieri1144889 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesFrankineaeGeodermatophilaceaeModestobacter
ProteomesiUP000006461: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei613 – 6131N6-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

Structurei

3D structure databases

ProteinModelPortaliI4ERQ3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni413 – 4186Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Phylogenomic databases

KOiK01895.

Family and domain databases

HAMAPiMF_01123. Ac_CoA_synth.
InterProiIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
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.

Sequencei

Sequence statusi: Complete.

I4ERQ3-1 [UniParc]FASTAAdd to Basket

« Hide

MSETTEAHGL TNPEGGFPPP EALAAAANVG PDVYDRAAAD RVGFWEEAAR    50
RLDWAQPWDQ ALDWSNPPFA KWFVGGKLNV AVNCVDRHVD AGHGDQVAYH 100
WIGEPGDTRT LTYAQLKDEV CKAANALVEL GVQAGDRVAI YLPMIPEAVV 150
AMLACARIGA VHMVVFGGFS PDALASRITD ADAKVVITAD GGYRRGAPSA 200
LKPNVDEALT KTEGVRSVLV VRRTETDVEW TEGRDVWWHE LVDRQPAEHE 250
AEAFDAEHPL YIMYTSGTTA KPKGILHTTG GYLTQVSYSH WAVFDIKPDT 300
DVFWTAADVG WVTGHSYIVY GPLSNRTTSV MYEGTPETPH RGRWWEIVQE 350
YGVTVLYTAP TTIRTFMKWG EDVPAGFDLS SLRLLGSVGE PINPEAWLWY 400
HTHIGGGRCP IVDTWWQTET GAHMITPLPA VTTLKPGSAQ RPLPGIAASV 450
VDEEGKPIEP GATGYLVLTE PWPAMLRTIW GDDDRYVDTY WSRYGQGVYF 500
AGDGAKLDED GDIWLLGRVD DVMNVSGHRI STTEVESALV SHPTVAEAAV 550
VGATDPTTGQ GIVAFVILRG DAVDSGEDLV KTLRQHVRKE IGPIASPRQI 600
MVVAELPKTR SGKIMRRLLR DVAENRELGD VTTLTDSSVM ELISSKLPSS 650
ASED 654
Length:654
Mass (Da):71,418
Last modified:September 5, 2012 - v1
Checksum:i51ECCF44189295FF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FO203431 Genomic DNA. Translation: CCH86066.1.
RefSeqiYP_006364565.1. NC_017955.1.

Genome annotation databases

EnsemblBacteriaiCCH86066; CCH86066; MODMU_0609.
GeneIDi13007694.
KEGGimmar:MODMU_0609.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FO203431 Genomic DNA. Translation: CCH86066.1 .
RefSeqi YP_006364565.1. NC_017955.1.

3D structure databases

ProteinModelPortali I4ERQ3.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CCH86066 ; CCH86066 ; MODMU_0609 .
GeneIDi 13007694.
KEGGi mmar:MODMU_0609.

Phylogenomic databases

KOi K01895.

Enzyme and pathway databases

BioCyci MMAR477641:GLGK-607-MONOMER.

Family and domain databases

HAMAPi MF_01123. Ac_CoA_synth.
InterProi IPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
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.
ProtoNeti Search...

Publicationsi

  1. "Genome sequence of radiation-resistant Modestobacter marinus strain BC501, a representative Actinobacterium that thrives on calcareous stone surfaces."
    Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L., Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A., Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.
    J. Bacteriol. 194:4773-4774(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BC501Imported.

Entry informationi

Entry nameiI4ERQ3_MODMB
AccessioniPrimary (citable) accession number: I4ERQ3
Entry historyi
Integrated into UniProtKB/TrEMBL: September 5, 2012
Last sequence update: September 5, 2012
Last modified: June 11, 2014
This is version 11 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

Similar proteinsi