Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

E8S8F1

- E8S8F1_MICSL

UniProt

E8S8F1 - E8S8F1_MICSL

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Micromonospora sp. (strain L5)
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 sitei310 – 3101Coenzyme AUniRule annotation
Binding sitei507 – 5071ATPUniRule annotation
Binding sitei522 – 5221ATPUniRule annotation
Binding sitei530 – 5301Coenzyme A; via carbonyl oxygenUniRule annotation
Metal bindingi544 – 5441Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi546 – 5461Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi549 – 5491Magnesium; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi386 – 3883ATPUniRule annotation
Nucleotide bindingi410 – 4156ATPUniRule 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

Enzyme and pathway databases

BioCyciMSP648999:GHVN-411-MONOMER.

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:ML5_0403Imported
OrganismiMicromonospora sp. (strain L5)Imported
Taxonomic identifieri648999 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicromonosporineaeMicromonosporaceaeMicromonospora
ProteomesiUP000008685: 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

Structurei

3D structure databases

ProteinModelPortaliE8S8F1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni192 – 1954Coenzyme A bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000229981.
KOiK01895.
OMAiAWIWYRD.

Family and domain databases

HAMAPiMF_01123. Ac_CoA_synth.
InterProiIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
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.

Sequencei

Sequence statusi: Complete.

E8S8F1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSEALANLLN ETRQFPPPAE LAANANVTAE AYEEAAGDRL AFWERQAGRL
60 70 80 90 100
AWAQPWEQVL DWSNAPFAKW FTGGRLNVAY NCLDRHVEAG LGDKVAIHWE
110 120 130 140 150
GEPGDTRTVT YADLHKLTCQ AANALTELGV TAGDRVAIYL PMIPEAAVAM
160 170 180 190 200
LACARIGATH SVVFGGFSAD ALTNRIQDAS AKVVITADGG FRRGKPSALK
210 220 230 240 250
PTVDEAVANC PSVEHVLVVR RTGEEVAWSA KDHWWHETVE TASPEHEAQA
260 270 280 290 300
FDAEHPLFIL YTSGTTARPK GILHTTGGYL TQTSYTTHAV FDLKPETDVY
310 320 330 340 350
WCTADIGWVT GHSYIVYGPL SNGATQVMYE GTPDTPHKGR FWEVVDKYKV
360 370 380 390 400
TILYTAPTLI RTMMKWGEDI PAGYDLSSLR LLGSVGEPIN PEAWIWYRQH
410 420 430 440 450
VGRGELPVVD TWWQTETGAI MISPLPGVTE AKPGSAMSPL PGIVADVVDD
460 470 480 490 500
QGQSVPNGGG GYLVLKEPWP SMLRTIWGDD NRFLETYWSR FGAGANTGDE
510 520 530 540 550
WVYFAGDGAK KDDDGHIWLL GRVDDVMLVS GHNISTTEVE SALVSHPSVA
560 570 580 590 600
EAAVVGATDP TTGQAIVAFA IPRGSAEISG DAGEQLIAEL RNHVAKTLGP
610 620 630 640 650
IAKPRQIMLV PELPKTRSGK IMRRLLRDVA ENRSLGDVTT LQDSSVMELI
660
SSGMSGGKSD ED
Length:662
Mass (Da):71,800
Last modified:April 5, 2011 - v1
Checksum:i31D50DC26ECEAAFB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002399 Genomic DNA. Translation: ADU05955.1.
RefSeqiWP_013473573.1. NC_014815.1.
YP_004080106.1. NC_014815.1.

Genome annotation databases

EnsemblBacteriaiADU05955; ADU05955; ML5_0403.
GeneIDi10055885.
KEGGimil:ML5_0403.
PATRICi45268612. VBIMicSp154089_0413.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002399 Genomic DNA. Translation: ADU05955.1 .
RefSeqi WP_013473573.1. NC_014815.1.
YP_004080106.1. NC_014815.1.

3D structure databases

ProteinModelPortali E8S8F1.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADU05955 ; ADU05955 ; ML5_0403 .
GeneIDi 10055885.
KEGGi mil:ML5_0403.
PATRICi 45268612. VBIMicSp154089_0413.

Phylogenomic databases

HOGENOMi HOG000229981.
KOi K01895.
OMAi AWIWYRD.

Enzyme and pathway databases

BioCyci MSP648999:GHVN-411-MONOMER.

Family and domain databases

HAMAPi MF_01123. Ac_CoA_synth.
InterProi IPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
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.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: L5Imported.

Entry informationi

Entry nameiE8S8F1_MICSL
AccessioniPrimary (citable) accession number: E8S8F1
Entry historyi
Integrated into UniProtKB/TrEMBL: April 5, 2011
Last sequence update: April 5, 2011
Last modified: November 26, 2014
This is version 26 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