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A4F6L2

- A4F6L2_SACEN

UniProt

A4F6L2 - A4F6L2_SACEN

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Protein
Acetyl-coenzyme A synthetase
Gene
acsA, SACE_0337
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 sitei317 – 3171Coenzyme A By similarityUniRule annotation
Binding sitei341 – 3411Coenzyme A By similarityUniRule annotation
Binding sitei393 – 3931Substrate; via nitrogen amide By similarityUniRule annotation
Binding sitei508 – 5081Substrate By similarityUniRule annotation
Binding sitei523 – 5231Substrate By similarityUniRule annotation
Active sitei525 – 5251 By similarityUniRule annotation
Binding sitei531 – 5311Coenzyme A By similarityUniRule annotation
Binding sitei534 – 5341Substrate By similarityUniRule annotation
Metal bindingi545 – 5451Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi547 – 5471Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi550 – 5501Magnesium; via carbonyl oxygen By similarityUniRule annotation
Binding sitei595 – 5951Coenzyme 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
Complete GO annotation...

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_0337Imported
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 residuei620 – 6201N6-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_0337.

Structurei

3D structure databases

ProteinModelPortaliA4F6L2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni417 – 4226Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiGGCEAVT.
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.

A4F6L2-1 [UniParc]FASTAAdd to Basket

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MSEPDGQSNT LDNLLTESRT FPPSGEFAAQ ANATSELYAQ ADADREAFWA    50
DQARHLHWDT EWEQVLDWSG APFAKWFVGG KLNVAYNCVD RHVEAGNGDR 100
VAIHWEGEPG DSRAITYAEL AREVSRTANA LASLGVGAGD RVAIYLPMLP 150
EAVYSMLACA RLGALHSVVF GGFSSEALRT RINDAQAKVV ITADGQYRRG 200
KAMPLKTNVD EAVAATPSVE HVLVVQRTKT DVEWNDGRDQ WWHDVVEGRP 250
ASHTPEFFDS EHPLFILYTS GTTGRPKGIL HTSGGYLTQA AYTHRTVFDL 300
KPETDVYWCT ADIGWVTGHT YIVYGPLANG ATQVIYEGTP NTPHEGRHWD 350
IVQKYGVTLY YTAPTTIRTF MKWGAEIPAR YDLSTLRVLG SVGEPINPEA 400
WMWYREHIGG NRAPIVDTWW QTETGAIMIS PLPGVTATKP GSAQVPLPGI 450
AAKVVDESGE QVGHGGGGLL VLDQPWPAML RGIWGDDDRY RETYWSKFAD 500
KGYYFAGDGA KYDDDGDIWL LGRVDDVMNV SGHRISTTEV ESALVSHPTV 550
AEAAVVGASD PTTGQGIVAF VILRGGADDQ ASGEAAIKAL RDHVAHEIGP 600
IAKPRQIMVV PELPKTRSGK IMRRLLRDVA ENREIGDVST LADSSVMDLI 650
SAGLGKSTED 660
Length:660
Mass (Da):72,043
Last modified:April 17, 2007 - v1
Checksum:iF986E6A54DAD71C8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM420293 Genomic DNA. Translation: CAL99686.1.
RefSeqiWP_011873025.1. NC_009142.1.
YP_001102612.1. NC_009142.1.

Genome annotation databases

EnsemblBacteriaiCAL99686; CAL99686; SACE_0337.
GeneIDi4940204.
KEGGisen:SACE_0337.
PATRICi23408036. VBISacEry28377_0340.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM420293 Genomic DNA. Translation: CAL99686.1 .
RefSeqi WP_011873025.1. NC_009142.1.
YP_001102612.1. NC_009142.1.

3D structure databases

ProteinModelPortali A4F6L2.
ModBasei Search...

Protein-protein interaction databases

STRINGi 405948.SACE_0337.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAL99686 ; CAL99686 ; SACE_0337 .
GeneIDi 4940204.
KEGGi sen:SACE_0337.
PATRICi 23408036. VBISacEry28377_0340.

Phylogenomic databases

eggNOGi COG0365.
HOGENOMi HOG000229981.
KOi K01895.
OMAi GGCEAVT.
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 nameiA4F6L2_SACEN
AccessioniPrimary (citable) accession number: A4F6L2
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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