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.

I4CUB2

- I4CUB2_PSEST

UniProt

I4CUB2 - I4CUB2_PSEST

(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, A458_12170
Organism
Pseudomonas stutzeri CCUG 29243
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 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: 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

BioCyciPSTU1196835:GLIX-2444-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 annotation
ORF Names:A458_12170Imported
OrganismiPseudomonas stutzeri CCUG 29243Imported
Taxonomic identifieri1196835 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000006063: 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

Structurei

3D structure databases

ProteinModelPortaliI4CUB2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni411 – 4166Substrate 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.
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.

I4CUB2-1 [UniParc]FASTAAdd to Basket

« Hide

MSAASVYPVR PEVAAQSLTN EASYKAMYQQ SVINPEGFWR EQAARLNWIR    50
PFTEVKRTSF DDHHVDIKWF ADGTLNVSAN CLDRHLAERG DQLAIIWEGD 100
DPSEHREITY RELHQEVSKF ANALRGQDVH RGDVVTIYMP MIPEAAVAML 150
ACARIGAIHS VVFGGFSPEA LAGRIIDGQS KIVITADEGV RGGKPVPLKG 200
NVDEALTNPQ TSCVKKIIVV RRTGADIRWH SHRDICYDDL MRVAGEVCAP 250
KEMGAEEPLF ILYTSGSTGK PKGVLHTCGG YLLYAALTHE RVFDYRPGEV 300
YWCTADIGWI TGHSYLIYGP LANGATTLMY EGVPNHPDVT RIARIIDKHK 350
VNILYTAPTA IRAMMAEGAA AVEGADGSSL RLLGTVGEPI NPEAWHWYYE 400
TVGQSRCPIV DTWWQTETGG ILISPLPGAT TLKPGSATRP MFGVVPGLVD 450
NLGNLLEGPA EGNLVILDSW PGQMRTIYKD HDRFVDTYFK TFRGMYFTGD 500
GARRDEDGYY WITGRVDDVL NVSGHRMGTA EIESAMVAHA KVAEAAAVGV 550
PHKLKGQAIY VYVTLVSGVQ PSDALRQELQ QWVRKEIGPI AVPDVIQWAP 600
GLPKTRSGKI MRRLLRKIAT DDYDALGDTS TLADPGVVDQ LIEAHEAVRK 650
R 651
Length:651
Mass (Da):71,716
Last modified:September 5, 2012 - v1
Checksum:iD85BB766C8B3B657
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003677 Genomic DNA. Translation: AFM33669.1.
RefSeqiWP_014820603.1. NC_018028.1.
YP_006458092.1. NC_018028.1.

Genome annotation databases

EnsemblBacteriaiAFM33669; AFM33669; A458_12170.
GeneIDi13145759.
KEGGipsc:A458_12170.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003677 Genomic DNA. Translation: AFM33669.1 .
RefSeqi WP_014820603.1. NC_018028.1.
YP_006458092.1. NC_018028.1.

3D structure databases

ProteinModelPortali I4CUB2.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AFM33669 ; AFM33669 ; A458_12170 .
GeneIDi 13145759.
KEGGi psc:A458_12170.

Phylogenomic databases

KOi K01895.

Enzyme and pathway databases

BioCyci PSTU1196835:GLIX-2444-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 Naphthalene-Degrading Bacterium Pseudomonas stutzeri AN10 (CCUG 29243)."
    Brunet-Galmes I., Busquets A., Pena A., Gomila M., Nogales B., Garcia-Valdes E., Lalucat J., Bennasar A., Bosch R.
    J. Bacteriol. 194:6642-6643(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CCUG 29243Imported.

Entry informationi

Entry nameiI4CUB2_PSEST
AccessioniPrimary (citable) accession number: I4CUB2
Entry historyi
Integrated into UniProtKB/TrEMBL: September 5, 2012
Last sequence update: September 5, 2012
Last modified: September 3, 2014
This is version 14 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