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A4F6L2

- A4F6L2_SACEN

UniProt

A4F6L2 - A4F6L2_SACEN

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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

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.UniRule annotation

Catalytic activityi

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

Cofactori

Note: Magnesium.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei317 – 3171Coenzyme AUniRule annotation
Binding sitei341 – 3411Coenzyme AUniRule annotation
Binding sitei508 – 5081ATPUniRule annotation
Binding sitei523 – 5231ATPUniRule annotation
Binding sitei531 – 5311Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei534 – 5341ATPUniRule annotation
Metal bindingi545 – 5451Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi547 – 5471Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi550 – 5501Magnesium; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi393 – 3953ATPUniRule annotation
Nucleotide bindingi417 – 4226ATPUniRule 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 ligaseUniRule annotation
Acyl-activating enzymeUniRule annotation
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-acetyllysineUniRule annotation

Post-translational modificationi

Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme.UniRule annotation

Keywords - PTMi

AcetylationUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi405948.SACE_0337.

Structurei

3D structure databases

ProteinModelPortaliA4F6L2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni198 – 2014Coenzyme A bindingUniRule annotation

Sequence similaritiesi

Belongs to the ATP-dependent AMP-binding enzyme family.UniRule annotation

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

« Hide

        10         20         30         40         50
MSEPDGQSNT LDNLLTESRT FPPSGEFAAQ ANATSELYAQ ADADREAFWA
60 70 80 90 100
DQARHLHWDT EWEQVLDWSG APFAKWFVGG KLNVAYNCVD RHVEAGNGDR
110 120 130 140 150
VAIHWEGEPG DSRAITYAEL AREVSRTANA LASLGVGAGD RVAIYLPMLP
160 170 180 190 200
EAVYSMLACA RLGALHSVVF GGFSSEALRT RINDAQAKVV ITADGQYRRG
210 220 230 240 250
KAMPLKTNVD EAVAATPSVE HVLVVQRTKT DVEWNDGRDQ WWHDVVEGRP
260 270 280 290 300
ASHTPEFFDS EHPLFILYTS GTTGRPKGIL HTSGGYLTQA AYTHRTVFDL
310 320 330 340 350
KPETDVYWCT ADIGWVTGHT YIVYGPLANG ATQVIYEGTP NTPHEGRHWD
360 370 380 390 400
IVQKYGVTLY YTAPTTIRTF MKWGAEIPAR YDLSTLRVLG SVGEPINPEA
410 420 430 440 450
WMWYREHIGG NRAPIVDTWW QTETGAIMIS PLPGVTATKP GSAQVPLPGI
460 470 480 490 500
AAKVVDESGE QVGHGGGGLL VLDQPWPAML RGIWGDDDRY RETYWSKFAD
510 520 530 540 550
KGYYFAGDGA KYDDDGDIWL LGRVDDVMNV SGHRISTTEV ESALVSHPTV
560 570 580 590 600
AEAAVVGASD PTTGQGIVAF VILRGGADDQ ASGEAAIKAL RDHVAHEIGP
610 620 630 640 650
IAKPRQIMVV PELPKTRSGK IMRRLLRDVA ENREIGDVST LADSSVMDLI
660
SAGLGKSTED
Length:660
Mass (Da):72,043
Last modified:April 17, 2007 - v1
Checksum:iF986E6A54DAD71C8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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...
MobiDBi 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 23338Imported.

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: November 26, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3