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I4CUB2

- I4CUB2_PSEST

UniProt

I4CUB2 - I4CUB2_PSEST

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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

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.UniRule annotation

Catalytic activityi

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

Cofactori

Note: 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: InterPro
Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotationImported

Keywords - Ligandi

ATP-bindingUniRule annotation, MagnesiumUniRule annotationSAAS annotation, Metal-bindingUniRule annotationSAAS annotation, 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 ligaseUniRule annotation
Acyl-activating enzymeUniRule annotation
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-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

ProteinModelPortaliI4CUB2.
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.

I4CUB2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSAASVYPVR PEVAAQSLTN EASYKAMYQQ SVINPEGFWR EQAARLNWIR
60 70 80 90 100
PFTEVKRTSF DDHHVDIKWF ADGTLNVSAN CLDRHLAERG DQLAIIWEGD
110 120 130 140 150
DPSEHREITY RELHQEVSKF ANALRGQDVH RGDVVTIYMP MIPEAAVAML
160 170 180 190 200
ACARIGAIHS VVFGGFSPEA LAGRIIDGQS KIVITADEGV RGGKPVPLKG
210 220 230 240 250
NVDEALTNPQ TSCVKKIIVV RRTGADIRWH SHRDICYDDL MRVAGEVCAP
260 270 280 290 300
KEMGAEEPLF ILYTSGSTGK PKGVLHTCGG YLLYAALTHE RVFDYRPGEV
310 320 330 340 350
YWCTADIGWI TGHSYLIYGP LANGATTLMY EGVPNHPDVT RIARIIDKHK
360 370 380 390 400
VNILYTAPTA IRAMMAEGAA AVEGADGSSL RLLGTVGEPI NPEAWHWYYE
410 420 430 440 450
TVGQSRCPIV DTWWQTETGG ILISPLPGAT TLKPGSATRP MFGVVPGLVD
460 470 480 490 500
NLGNLLEGPA EGNLVILDSW PGQMRTIYKD HDRFVDTYFK TFRGMYFTGD
510 520 530 540 550
GARRDEDGYY WITGRVDDVL NVSGHRMGTA EIESAMVAHA KVAEAAAVGV
560 570 580 590 600
PHKLKGQAIY VYVTLVSGVQ PSDALRQELQ QWVRKEIGPI AVPDVIQWAP
610 620 630 640 650
GLPKTRSGKI MRRLLRKIAT DDYDALGDTS TLADPGVVDQ LIEAHEAVRK

R
Length:651
Mass (Da):71,716
Last modified:September 5, 2012 - v1
Checksum:iD85BB766C8B3B657
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003677 Genomic DNA. Translation: AFM33669.1.
RefSeqiYP_006458092.1. NC_018028.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003677 Genomic DNA. Translation: AFM33669.1 .
RefSeqi 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: November 26, 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