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A4FCA0

- A4FCA0_SACEN

UniProt

A4FCA0 - A4FCA0_SACEN

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Protein

Acetyl-coenzyme A synthetase

Gene
acsA, SACE_2375
Organism
Saccharopolyspora erythraea (strain NRRL 23338)
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 annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei325 – 3251Coenzyme A By similarityUniRule annotation
Binding sitei349 – 3491Coenzyme A By similarityUniRule annotation
Binding sitei401 – 4011Substrate; via nitrogen amide By similarityUniRule annotation
Binding sitei516 – 5161Substrate By similarityUniRule annotation
Binding sitei531 – 5311Substrate By similarityUniRule annotation
Active sitei533 – 5331 By similarityUniRule annotation
Binding sitei539 – 5391Coenzyme A By similarityUniRule annotation
Binding sitei542 – 5421Substrate By similarityUniRule annotation
Metal bindingi553 – 5531Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi555 – 5551Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi558 – 5581Magnesium; via carbonyl oxygen By similarityUniRule annotation
Binding sitei603 – 6031Coenzyme 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 annotation, Metal-bindingUniRule 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 ligase
Acyl-activating enzyme
Gene namesi
Name:acsAUniRule annotationImported
Ordered Locus Names:SACE_2375Imported
OrganismiSaccharopolyspora erythraea (strain NRRL 23338)Imported
Taxonomic identifieri405948 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesPseudonocardineaePseudonocardiaceaeSaccharopolyspora
ProteomesiUP000006728: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei628 – 6281N6-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

Interactioni

Protein-protein interaction databases

STRINGi405948.SACE_2375.

Structurei

3D structure databases

ProteinModelPortaliA4FCA0.
SMRiA4FCA0. Positions 29-641.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni425 – 4306Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiKMEHLRI.
OrthoDBiEOG68WR2H.

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.

A4FCA0-1 [UniParc]FASTAAdd to Basket

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MSSKRVERLE VGKHSQNTLD NLLHEERIHA PSGEFAAQAN ATSELYAQAD    50
ADREAFWADQ ARHLHWDTEW EQVLDWSGAP FAKWFVGGKL NVAYNCVDRH 100
VEAGNGDRVA IHWEGEPGDS RAITYAELAR EVSRTANALA SLGVGAGDRV 150
AIYLPMLPEA VYSMLACARL GALHSVVFGG FSSEALRTRI NDAQAKVVIT 200
ADGQYRRGKA MPLKTNVDEA VAATPSVEHV LVVQRTKTDV EWNDGRDQWW 250
HDVVEGRPAS HTPEFFDSEH PLFILYTSGT TGRPKGILHT SGGYLTQAAY 300
THRTVFDLKP ETDVYWCTAD IGWVTGHTYI VYGPLANGAT QVIYEGTPNT 350
PHEGRHWDIV QKYGVTLYYT APTTIRTFMK WGAEIPARYD LSTLRVLGSV 400
GEPINPEAWM WYREHIGGNR APIVDTWWQT ETGAIMISPL PGVTATKPGS 450
AQVPLPGIAA KVVDESGEQV GHGGGGLLVL DQPWPAMLRG IWGDDDRYRE 500
TYWSKFADKG YYFAGDGAKY DDDGDIWLLG RVDDVMNVSG HRISTTEVES 550
ALVSHPTVAE AAVVGASDPT TGQGIVAFVI LRGGADDQAS GEAAIKALRD 600
HVAHEIGPIA KPRQIMVVPE LPKTRSGKIM RRLLRDVAEN REIGDVSTLA 650
DSSVMNLISA GFATSSDD 668
Length:668
Mass (Da):73,110
Last modified:April 17, 2007 - v1
Checksum:iC7663AB223D18862
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM420293 Genomic DNA. Translation: CAM01675.1.
RefSeqiWP_011873661.1. NC_009142.1.
YP_001104600.1. NC_009142.1.

Genome annotation databases

EnsemblBacteriaiCAM01675; CAM01675; SACE_2375.
GeneIDi4942224.
KEGGisen:SACE_2375.
PATRICi23412162. VBISacEry28377_2375.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM420293 Genomic DNA. Translation: CAM01675.1 .
RefSeqi WP_011873661.1. NC_009142.1.
YP_001104600.1. NC_009142.1.

3D structure databases

ProteinModelPortali A4FCA0.
SMRi A4FCA0. Positions 29-641.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 405948.SACE_2375.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAM01675 ; CAM01675 ; SACE_2375 .
GeneIDi 4942224.
KEGGi sen:SACE_2375.
PATRICi 23412162. VBISacEry28377_2375.

Phylogenomic databases

eggNOGi COG0365.
HOGENOMi HOG000229981.
KOi K01895.
OMAi KMEHLRI.
OrthoDBi EOG68WR2H.

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 erythromycin-producing bacterium Saccharopolyspora erythraea NRRL23338."
    Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S., Haydock S.F., Leadlay P.F.
    Nat. Biotechnol. 25:447-453(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NRRL 23338.

Entry informationi

Entry nameiA4FCA0_SACEN
AccessioniPrimary (citable) accession number: A4FCA0
Entry historyi
Integrated into UniProtKB/TrEMBL: April 17, 2007
Last sequence update: April 17, 2007
Last modified: September 3, 2014
This is version 50 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

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