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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Burkholderia ambifaria (strain MC40-6)
Status
Unreviewed-Annotation score: 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

Mg2+UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei321Coenzyme AUniRule annotation1
Binding sitei516ATPUniRule annotation1
Binding sitei532ATPUniRule annotation1
Binding sitei540Coenzyme A; via carbonyl oxygenUniRule annotation1
Binding sitei543ATPUniRule annotation1
Metal bindingi554Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi556Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi559Magnesium; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi401 – 403ATPUniRule annotation3
Nucleotide bindingi425 – 430ATPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

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 annotation
Ordered Locus Names:BamMC406_5891Imported
OrganismiBurkholderia ambifaria (strain MC40-6)Imported
Taxonomic identifieri398577 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex
Proteomesi
  • UP000001680 Componenti: Chromosome 3

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei629N6-acetyllysineUniRule annotation1

Post-translational modificationi

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

Keywords - PTMi

AcetylationUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB1Z3L5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini36 – 91ACAS_NInterPro annotationAdd BLAST56
Domaini98 – 539AMP-bindingInterPro annotationAdd BLAST442
Domaini548 – 629AMP-binding_CInterPro annotationAdd BLAST82

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni201 – 204Coenzyme A bindingUniRule annotation4

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000229981.
KOiK01895.
OMAiGPLANGC.
OrthoDBiPOG091H059D.

Family and domain databases

CDDicd05966. ACS. 1 hit.
HAMAPiMF_01123. Ac_CoA_synth. 1 hit.
InterProiIPR011904. Ac_CoA_lig.
IPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. 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.

B1Z3L5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENTLTAIVS ILQERRIFEP TADTRERATI SGMPAYQALA AEAERDYEGF
60 70 80 90 100
WARLAREGLS WHKPFTKVLD ESDAPFYKWF DDGELNASYN CLDRHVEAGN
110 120 130 140 150
GERVAVIFEA DDGTVTRVTY ADLLARVSRF ANALKKRGIA KGDRVVIYMP
160 170 180 190 200
MSIEGIVAMQ ACARIGATHS VVFGGFSAKS LNERLVDVGA VALITADEQA
210 220 230 240 250
RGGKTLPLKS IADEAIAMGG CEAVKSVIVY RRTGGKVDWH AGRDLWMHEL
260 270 280 290 300
AHAESDTCAP EWVGAEHPLF ILYTSGSTGK PKGVQHSTGG YLLWAAQTMK
310 320 330 340 350
WTFDWKPTDV FWCTADIGWV TGHTYITYGP LACGGTQVVF EGVPTYPDAG
360 370 380 390 400
RFWKMIADHK VTVFYTAPTA IRSLIKAAEA DDKVHPKSYD LSSLRIIGTV
410 420 430 440 450
GEPINPEAWM WYHKHVGQER CPIVDTWWQT ETGGHMITPL PGATPTVPGS
460 470 480 490 500
CTLPLPGIMA AVVDETGQDV PNGQGGILVV KRPWPAMIRT IWGDPERFKK
510 520 530 540 550
SYYPEELGGR LYLAGDGTVR DKDTGYFTIM GRIDDVLNVS GHRLGTMEIE
560 570 580 590 600
SALVSHELVA EAAVVGRPDD TTGEAVVAFV VLKRSRPEGE EAAALAKTLR
610 620 630 640 650
DWVGKQIGPI AKPKDIRFGD NLPKTRSGKI MRRLLRSLAK GEAITQDTST
660
LENPAILDQL GQSL
Length:664
Mass (Da):72,777
Last modified:May 20, 2008 - v1
Checksum:i208A8B2F4243E6FD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001027 Genomic DNA. Translation: ACB68328.1.

Genome annotation databases

EnsemblBacteriaiACB68328; ACB68328; BamMC406_5891.
KEGGibac:BamMC406_5891.
PATRICi19042153. VBIBurAmb82852_6352.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001027 Genomic DNA. Translation: ACB68328.1.

3D structure databases

ProteinModelPortaliB1Z3L5.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACB68328; ACB68328; BamMC406_5891.
KEGGibac:BamMC406_5891.
PATRICi19042153. VBIBurAmb82852_6352.

Phylogenomic databases

HOGENOMiHOG000229981.
KOiK01895.
OMAiGPLANGC.
OrthoDBiPOG091H059D.

Family and domain databases

CDDicd05966. ACS. 1 hit.
HAMAPiMF_01123. Ac_CoA_synth. 1 hit.
InterProiIPR011904. Ac_CoA_lig.
IPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiB1Z3L5_BURA4
AccessioniPrimary (citable) accession number: B1Z3L5
Entry historyi
Integrated into UniProtKB/TrEMBL: May 20, 2008
Last sequence update: May 20, 2008
Last modified: November 2, 2016
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.