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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei316 – 3161Coenzyme AUniRule annotation
Binding sitei508 – 5081ATPUniRule annotation
Binding sitei523 – 5231ATPUniRule annotation
Binding sitei531 – 5311Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei534 – 5341ATPUniRule annotation
Metal bindingi545 – 5451Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi547 – 5471Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi550 – 5501Magnesium; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi392 – 3943ATPUniRule annotation
Nucleotide bindingi416 – 4216ATPUniRule 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

Ligase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciNEUT335283:GHT6-1724-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:Neut_1690
OrganismiNitrosomonas eutropha (strain C91)
Taxonomic identifieri335283 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas
ProteomesiUP000001966: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 655655Acetyl-coenzyme A synthetasePRO_1000065298Add
BLAST

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

Acetylation

Interactioni

Protein-protein interaction databases

STRINGi335283.Neut_1690.

Structurei

3D structure databases

ProteinModelPortaliQ0AFF1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni196 – 1994Coenzyme A bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiAWEWYFE.
OrthoDBiEOG68WR2H.

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.

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.
RefSeqiYP_747896.1. NC_008344.1.

Genome annotation databases

EnsemblBacteriaiABI59931; ABI59931; Neut_1690.
GeneIDi4273573.
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.
RefSeqiYP_747896.1. 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.
GeneIDi4273573.
KEGGinet:Neut_1690.
PATRICi22720832. VBINitEut7577_2068.

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiAWEWYFE.
OrthoDBiEOG68WR2H.

Enzyme and pathway databases

BioCyciNEUT335283:GHT6-1724-MONOMER.

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.
ProtoNetiSearch...

Publicationsi

  1. "Whole-genome analysis of the ammonia-oxidizing bacterium, Nitrosomonas eutropha C91: implications for niche adaptation."
    Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S., Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., Wei X.
    Environ. Microbiol. 9:2993-3007(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C91.

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: February 4, 2015
This is version 61 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.