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K0CWU1

- K0CWU1_ALTME

UniProt

K0CWU1 - K0CWU1_ALTME

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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Alteromonas macleodii (strain English Channel 673)
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

Magnesium.UniRule annotationSAAS annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei311 – 3111Coenzyme 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 annotation

Keywords - Ligandi

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

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
Ordered Locus Names:AMEC673_16675Imported
OrganismiAlteromonas macleodii (strain English Channel 673)Imported
Taxonomic identifieri1004788 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeAlteromonas
ProteomesiUP000006296: 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

ProteinModelPortaliK0CWU1.
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.
OMAiDISWING.

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.

K0CWU1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTASKTYPVP ENILQSTHLT ASQYDEMYKQ SVEQPEAFWA EHASMLEWYQ
60 70 80 90 100
KPTKIKNTMF GENDVSIKWF EDGELNASYN CIDRHLADNA TKVAFHWEGD
110 120 130 140 150
SPEDSQDITY QQVHYEVCKL ANALKEMGVA KGDRVAIYMP MVPEAAYAML
160 170 180 190 200
ACARIGAVHS VIFGGFSPNA IADRINDSNA KVVITADEGR RAGRSIPLKA
210 220 230 240 250
NVDKALAGDA CPSITHVLVH KLTGGDVDWN AKHDVWWHDA VDGVSAQCEP
260 270 280 290 300
EVMNAEDPLF ILYTSGSTGT PKGVVHTTGG YLLYSAMTFK YAFDYKEDDV
310 320 330 340 350
YWCTADVGWI TGHSYMVYGP MVNAASQVFF EGVPTYPDVK RIAQVVEKYK
360 370 380 390 400
VNSLYTAPTA IRALMAHGDV PTEGCDVSSL RLLGTVGEPI NPEAWEWYHR
410 420 430 440 450
VIGMSRCPII DTWWQTETGG HMILPLPGAT ELKPGSATRP FFGIQPALFD
460 470 480 490 500
ADGNELEGAA EGNLVIKDSW PSQARTVYGD HQRFINTYFS AYKGVYFTGD
510 520 530 540 550
GARCDEDGFY WITGRVDDVL NVSGHRLGTA EIESALVAHP KVAEAAVVGF
560 570 580 590 600
PHDIKGQGIY VYVTPNEGVE ANEALTKELK AWVRQELSPI ATPDMIQWSR
610 620 630 640
GLPKTRSGKI MRRILRKIAA NEHEQLGDTS TLADPSVVDT LIEERLNK
Length:648
Mass (Da):71,668
Last modified:November 28, 2012 - v1
Checksum:iB044EA01F57280B0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003844 Genomic DNA. Translation: AFT76017.1.
RefSeqiYP_006800394.1. NC_018678.1.

Genome annotation databases

EnsemblBacteriaiAFT76017; AFT76017; AMEC673_16675.
GeneIDi13741805.
KEGGiamg:AMEC673_16675.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003844 Genomic DNA. Translation: AFT76017.1 .
RefSeqi YP_006800394.1. NC_018678.1.

3D structure databases

ProteinModelPortali K0CWU1.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AFT76017 ; AFT76017 ; AMEC673_16675 .
GeneIDi 13741805.
KEGGi amg:AMEC673_16675.

Phylogenomic databases

KOi K01895.
OMAi DISWING.

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. "Genomes of surface isolates of Alteromonas macleodii: the life of a widespread marine opportunistic copiotroph."
    Lopez-Perez M., Gonzaga A., Martin-Cuadrado A.B., Onyshchenko O., Ghavidel A., Ghai R., Rodriguez-Valera F.
    Sci. Rep. 2:696-696(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: English Channel 673Imported.

Entry informationi

Entry nameiK0CWU1_ALTME
AccessioniPrimary (citable) accession number: K0CWU1
Entry historyi
Integrated into UniProtKB/TrEMBL: November 28, 2012
Last sequence update: November 28, 2012
Last modified: October 29, 2014
This is version 12 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