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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Modestobacter marinus
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 sitei313Coenzyme AUniRule annotation1
Binding sitei503ATPUniRule annotation1
Binding sitei518ATPUniRule annotation1
Binding sitei526Coenzyme A; via carbonyl oxygenUniRule annotation1
Binding sitei529ATPUniRule annotation1
Metal bindingi540Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi542Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi545Magnesium; via carbonyl oxygenUniRule annotation1
Binding sitei588Coenzyme AUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi389 – 391ATPUniRule annotation3
Nucleotide bindingi413 – 418ATPUniRule 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 annotationImported
Ordered Locus Names:MODMU_0609Imported
OrganismiModestobacter marinusImported
Taxonomic identifieri477641 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaGeodermatophilalesGeodermatophilaceaeModestobacter
Proteomesi
  • UP000006461 Componenti: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei613N6-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

ProteinModelPortaliI4ERQ3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini32 – 84ACAS_NInterPro annotationAdd BLAST53
Domaini90 – 525AMP-bindingInterPro annotationAdd BLAST436
Domaini534 – 613AMP-binding_CInterPro annotationAdd BLAST80

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni194 – 197Coenzyme A bindingUniRule annotation4

Sequence similaritiesi

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

Phylogenomic databases

KOiK01895.
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.
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.

Sequencei

Sequence statusi: Complete.

I4ERQ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSETTEAHGL TNPEGGFPPP EALAAAANVG PDVYDRAAAD RVGFWEEAAR
60 70 80 90 100
RLDWAQPWDQ ALDWSNPPFA KWFVGGKLNV AVNCVDRHVD AGHGDQVAYH
110 120 130 140 150
WIGEPGDTRT LTYAQLKDEV CKAANALVEL GVQAGDRVAI YLPMIPEAVV
160 170 180 190 200
AMLACARIGA VHMVVFGGFS PDALASRITD ADAKVVITAD GGYRRGAPSA
210 220 230 240 250
LKPNVDEALT KTEGVRSVLV VRRTETDVEW TEGRDVWWHE LVDRQPAEHE
260 270 280 290 300
AEAFDAEHPL YIMYTSGTTA KPKGILHTTG GYLTQVSYSH WAVFDIKPDT
310 320 330 340 350
DVFWTAADVG WVTGHSYIVY GPLSNRTTSV MYEGTPETPH RGRWWEIVQE
360 370 380 390 400
YGVTVLYTAP TTIRTFMKWG EDVPAGFDLS SLRLLGSVGE PINPEAWLWY
410 420 430 440 450
HTHIGGGRCP IVDTWWQTET GAHMITPLPA VTTLKPGSAQ RPLPGIAASV
460 470 480 490 500
VDEEGKPIEP GATGYLVLTE PWPAMLRTIW GDDDRYVDTY WSRYGQGVYF
510 520 530 540 550
AGDGAKLDED GDIWLLGRVD DVMNVSGHRI STTEVESALV SHPTVAEAAV
560 570 580 590 600
VGATDPTTGQ GIVAFVILRG DAVDSGEDLV KTLRQHVRKE IGPIASPRQI
610 620 630 640 650
MVVAELPKTR SGKIMRRLLR DVAENRELGD VTTLTDSSVM ELISSKLPSS

ASED
Length:654
Mass (Da):71,418
Last modified:September 5, 2012 - v1
Checksum:i51ECCF44189295FF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO203431 Genomic DNA. Translation: CCH86066.1.
RefSeqiWP_014738676.1. NC_017955.1.

Genome annotation databases

EnsemblBacteriaiCCH86066; CCH86066; MODMU_0609.
KEGGimmar:MODMU_0609.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO203431 Genomic DNA. Translation: CCH86066.1.
RefSeqiWP_014738676.1. NC_017955.1.

3D structure databases

ProteinModelPortaliI4ERQ3.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCH86066; CCH86066; MODMU_0609.
KEGGimmar:MODMU_0609.

Phylogenomic databases

KOiK01895.
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.
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.
ProtoNetiSearch...

Entry informationi

Entry nameiI4ERQ3_9ACTN
AccessioniPrimary (citable) accession number: I4ERQ3
Entry historyi
Integrated into UniProtKB/TrEMBL: September 5, 2012
Last sequence update: September 5, 2012
Last modified: November 2, 2016
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference 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.