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A4FCA0

- A4FCA0_SACEN

UniProt

A4FCA0 - A4FCA0_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 sitei325 – 3251Coenzyme AUniRule annotation
Binding sitei349 – 3491Coenzyme AUniRule annotation
Binding sitei516 – 5161ATPUniRule annotation
Binding sitei531 – 5311ATPUniRule annotation
Binding sitei539 – 5391Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei542 – 5421ATPUniRule annotation
Metal bindingi553 – 5531Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi555 – 5551Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi558 – 5581Magnesium; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi401 – 4033ATPUniRule annotation
Nucleotide bindingi425 – 4306ATPUniRule 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_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-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_2375.

Structurei

3D structure databases

ProteinModelPortaliA4FCA0.
SMRiA4FCA0. Positions 29-641.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni206 – 2094Coenzyme A bindingUniRule annotation

Sequence similaritiesi

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

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

« Hide

        10         20         30         40         50
MSSKRVERLE VGKHSQNTLD NLLHEERIHA PSGEFAAQAN ATSELYAQAD
60 70 80 90 100
ADREAFWADQ ARHLHWDTEW EQVLDWSGAP FAKWFVGGKL NVAYNCVDRH
110 120 130 140 150
VEAGNGDRVA IHWEGEPGDS RAITYAELAR EVSRTANALA SLGVGAGDRV
160 170 180 190 200
AIYLPMLPEA VYSMLACARL GALHSVVFGG FSSEALRTRI NDAQAKVVIT
210 220 230 240 250
ADGQYRRGKA MPLKTNVDEA VAATPSVEHV LVVQRTKTDV EWNDGRDQWW
260 270 280 290 300
HDVVEGRPAS HTPEFFDSEH PLFILYTSGT TGRPKGILHT SGGYLTQAAY
310 320 330 340 350
THRTVFDLKP ETDVYWCTAD IGWVTGHTYI VYGPLANGAT QVIYEGTPNT
360 370 380 390 400
PHEGRHWDIV QKYGVTLYYT APTTIRTFMK WGAEIPARYD LSTLRVLGSV
410 420 430 440 450
GEPINPEAWM WYREHIGGNR APIVDTWWQT ETGAIMISPL PGVTATKPGS
460 470 480 490 500
AQVPLPGIAA KVVDESGEQV GHGGGGLLVL DQPWPAMLRG IWGDDDRYRE
510 520 530 540 550
TYWSKFADKG YYFAGDGAKY DDDGDIWLLG RVDDVMNVSG HRISTTEVES
560 570 580 590 600
ALVSHPTVAE AAVVGASDPT TGQGIVAFVI LRGGADDQAS GEAAIKALRD
610 620 630 640 650
HVAHEIGPIA KPRQIMVVPE LPKTRSGKIM RRLLRDVAEN REIGDVSTLA
660
DSSVMNLISA GFATSSDD
Length:668
Mass (Da):73,110
Last modified:April 17, 2007 - v1
Checksum:iC7663AB223D18862
GO

Sequence databases

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

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: 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