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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Rhizobium loti (strain MAFF303099) (Mesorhizobium loti)
Status
Reviewed-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 sitei312Coenzyme AUniRule annotation1
Binding sitei336Coenzyme AUniRule annotation1
Binding sitei501ATPUniRule annotation1
Binding sitei516ATPUniRule annotation1
Binding sitei524Coenzyme A; via carbonyl oxygenUniRule annotation1
Binding sitei527ATPUniRule annotation1
Metal bindingi538Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi540Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi543Magnesium; via carbonyl oxygenUniRule annotation1
Binding sitei585Coenzyme AUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi388 – 390ATPUniRule annotation3
Nucleotide bindingi412 – 417ATPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, 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:mlr4089
OrganismiRhizobium loti (strain MAFF303099) (Mesorhizobium loti)
Taxonomic identifieri266835 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium
Proteomesi
  • UP000000552 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002083801 – 651Acetyl-coenzyme A synthetaseAdd BLAST651

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei610N6-acetyllysineUniRule annotation1

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Interactioni

Protein-protein interaction databases

STRINGi266835.mlr4089.

Structurei

3D structure databases

ProteinModelPortaliQ98ET8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni190 – 193Coenzyme A bindingUniRule annotation4

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
KOiK01895.
OMAiEGAPNWP.
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.

Q98ET8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEVHVHRVQ PAWKKNALID NDTYLKWYAD SIKNPDKFWG KHGKRIDWFK
60 70 80 90 100
PFSKVKNTSF DGKVSIKWFE DGLTNVSYNC IDRHLKKRGD QTAIIWEGDN
110 120 130 140 150
PYDDKKITYN ELYERVCRLA NVMKKHGVKK GDRVTIYMPM IPEAAYAMLA
160 170 180 190 200
CTRIGAIHSI VFGGFSPDAL AGRIVDCEST FVITADEGLR GGKSIPLKEN
210 220 230 240 250
TDKAIDIAAK NFVMVKNVLV VRRTGGKVGW APGRDLWYHD EVATVKAECK
260 270 280 290 300
PEKMKAEDPL FILYTSGSTG KPKGVLHTTA GYLVYASMTH QYVFDYHDGD
310 320 330 340 350
IYWCTADVGW VTGHSYIVYG PLANGATTLM FEGVPNYPSQ SRFWEVIDKH
360 370 380 390 400
KVNIFYTAPT ALRALMGAGN DPVKKTSRKS LRVLGSVGEP INPEAWEWYF
410 420 430 440 450
NVVGNGKVPI VDTWWQTETG GILITPLPGA TDLKAGSATR PFFGVKPQLV
460 470 480 490 500
DGEGKVLEGA ADGNLCITDS WPGQMRTVYG DHDRFVQTYF STYKGKYFTG
510 520 530 540 550
DGCRRDADGY YWITGRVDDV INVSGHRMGT AEVESALVSH DKVSEAAVVG
560 570 580 590 600
YPHDIKGQGI YSYVTLMKGE EPTEDLRKEL IAHVRKEIGA IASPDKIQFA
610 620 630 640 650
PGLPKTRSGK IMRRILRKIA EDDFSTLGDT STLADPAVVD DLIANRQNKK

G
Length:651
Mass (Da):72,530
Last modified:October 1, 2001 - v1
Checksum:iC7A0AC5011C4D43F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000012 Genomic DNA. Translation: BAB50829.1.
RefSeqiWP_010912172.1. NC_002678.2.

Genome annotation databases

EnsemblBacteriaiBAB50829; BAB50829; BAB50829.
GeneIDi1227704.
KEGGimlo:mlr4089.
PATRICi22480693. VBIMesLot2464_3234.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000012 Genomic DNA. Translation: BAB50829.1.
RefSeqiWP_010912172.1. NC_002678.2.

3D structure databases

ProteinModelPortaliQ98ET8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi266835.mlr4089.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB50829; BAB50829; BAB50829.
GeneIDi1227704.
KEGGimlo:mlr4089.
PATRICi22480693. VBIMesLot2464_3234.

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
KOiK01895.
OMAiEGAPNWP.
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 nameiACSA_RHILO
AccessioniPrimary (citable) accession number: Q98ET8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: October 1, 2001
Last modified: November 2, 2016
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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.