Skip Header

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

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Nitrosomonas eutropha (strain C91)
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 sitei316Coenzyme AUniRule annotation1
Binding sitei508ATPUniRule annotation1
Binding sitei523ATPUniRule annotation1
Binding sitei531Coenzyme A; via carbonyl oxygenUniRule annotation1
Binding sitei534ATPUniRule annotation1
Metal bindingi545Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi547Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi550Magnesium; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi392 – 394ATPUniRule annotation3
Nucleotide bindingi416 – 421ATPUniRule 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:Neut_1690
OrganismiNitrosomonas eutropha (strain C91)
Taxonomic identifieri335283 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas
Proteomesi
  • UP000001966 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000652981 – 655Acetyl-coenzyme A synthetaseAdd BLAST655

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei620N6-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

STRINGi335283.Neut_1690.

Structurei

3D structure databases

ProteinModelPortaliQ0AFF1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni196 – 199Coenzyme A bindingUniRule annotation4

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
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.
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.

Q0AFF1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATIESILRE NRIFPPANEF VRHANITGMK TYEALRQEAE RDYAGFWAKL
60 70 80 90 100
AKQYITWHKP FTRILDDTNP PFYKWFDDGE LNISWNCLDR HLTTQANKTA
110 120 130 140 150
IIFESDEGEV IRCSYRELHQ RVCRFANGLK ALGIRQGDRI VIYMPMRIEA
160 170 180 190 200
VVAMQACARI GVIHSVVFGG FSAKSVYERI IDAGASAVIT ADEQTRGGKR
210 220 230 240 250
HALKATVDEA LAMGDTTSVH SVIVFRHTGT DIPWQPERDR WWHNLTASQS
260 270 280 290 300
DECEPIWVNA EHPLFTLYTS GSTGKPKGVQ HSSAGYLLGA IVSMQWVFDY
310 320 330 340 350
HSEDIFWCTA DVGWVTGHSY VTYGPLAIGA TQVIFEGTPT YPHAGRFWEI
360 370 380 390 400
IQKHRVTTFY TAPTAIRSLI KLGPDLPEKY DLSSLRLLGS VGEPINPEAW
410 420 430 440 450
MWYYTVIGQS RCPVVDTWWQ TETGSHMIAP IPGAIPAKPG SCTLPLPGID
460 470 480 490 500
AAVVDETGLP AEQGKGGFLV IKRPFPSMLR TLWNDPERFR NTYFPADIAG
510 520 530 540 550
GHYYLAGDSA HRDQDGYFWI MGRIDDVLNV SGHRLGTMEI ESALVAHPLV
560 570 580 590 600
AEAAVVGKPH EIRGEVIVAF VVLRGKLPDD QQAAEIAETL REWVSSEIGA
610 620 630 640 650
IARPEEIRFG ENLPKTRSGK LMRRLLRSLA RGETITQDIS TLENPVILEQ

FSQTI
Length:655
Mass (Da):73,338
Last modified:October 17, 2006 - v1
Checksum:iB81E66505C045F43
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000450 Genomic DNA. Translation: ABI59931.1.
RefSeqiWP_011634737.1. NC_008344.1.

Genome annotation databases

EnsemblBacteriaiABI59931; ABI59931; Neut_1690.
KEGGinet:Neut_1690.
PATRICi22720832. VBINitEut7577_2068.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000450 Genomic DNA. Translation: ABI59931.1.
RefSeqiWP_011634737.1. NC_008344.1.

3D structure databases

ProteinModelPortaliQ0AFF1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi335283.Neut_1690.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABI59931; ABI59931; Neut_1690.
KEGGinet:Neut_1690.
PATRICi22720832. VBINitEut7577_2068.

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
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.
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 nameiACSA_NITEC
AccessioniPrimary (citable) accession number: Q0AFF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 17, 2006
Last modified: November 2, 2016
This is version 69 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.