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Q0AFF1

- ACSA_NITEC

UniProt

Q0AFF1 - ACSA_NITEC

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Protein
Acetyl-coenzyme A synthetase
Gene
acsA, Neut_1690
Organism
Nitrosomonas eutropha (strain C91)
Status
Reviewed - Annotation score: 4 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 By similarity.UniRule annotation

Catalytic activityi

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.UniRule annotation

Cofactori

Magnesium By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei316 – 3161Coenzyme A By similarity
Binding sitei392 – 3921Substrate; via amide nitrogen By similarity
Binding sitei508 – 5081Substrate By similarity
Binding sitei523 – 5231Substrate By similarity
Active sitei525 – 5251 By similarity
Binding sitei531 – 5311Coenzyme A By similarity
Binding sitei534 – 5341Substrate By similarity
Metal bindingi545 – 5451Magnesium; via carbonyl oxygen By similarity
Metal bindingi547 – 5471Magnesium; via carbonyl oxygen By similarity
Metal bindingi550 – 5501Magnesium; via carbonyl oxygen By similarity
Binding sitei595 – 5951Coenzyme A

GO - Molecular functioni

  1. AMP binding Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. acetate-CoA ligase activity Source: UniProtKB-HAMAP
  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 synthetase (EC:6.2.1.1)
Short name:
AcCoA synthetase
Short name:
Acs
Alternative name(s):
Acetate--CoA ligase
Acyl-activating enzyme
Gene namesi
Name:acsA
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 synthetaseUniRule annotation
PRO_1000065298Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei620 – 6201N6-acetyllysine By similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Interactioni

Protein-protein interaction databases

STRINGi335283.Neut_1690.

Structurei

3D structure databases

ProteinModelPortaliQ0AFF1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni416 – 4216Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiYNNDERF.
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

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MATIESILRE NRIFPPANEF VRHANITGMK TYEALRQEAE RDYAGFWAKL    50
AKQYITWHKP FTRILDDTNP PFYKWFDDGE LNISWNCLDR HLTTQANKTA 100
IIFESDEGEV IRCSYRELHQ RVCRFANGLK ALGIRQGDRI VIYMPMRIEA 150
VVAMQACARI GVIHSVVFGG FSAKSVYERI IDAGASAVIT ADEQTRGGKR 200
HALKATVDEA LAMGDTTSVH SVIVFRHTGT DIPWQPERDR WWHNLTASQS 250
DECEPIWVNA EHPLFTLYTS GSTGKPKGVQ HSSAGYLLGA IVSMQWVFDY 300
HSEDIFWCTA DVGWVTGHSY VTYGPLAIGA TQVIFEGTPT YPHAGRFWEI 350
IQKHRVTTFY TAPTAIRSLI KLGPDLPEKY DLSSLRLLGS VGEPINPEAW 400
MWYYTVIGQS RCPVVDTWWQ TETGSHMIAP IPGAIPAKPG SCTLPLPGID 450
AAVVDETGLP AEQGKGGFLV IKRPFPSMLR TLWNDPERFR NTYFPADIAG 500
GHYYLAGDSA HRDQDGYFWI MGRIDDVLNV SGHRLGTMEI ESALVAHPLV 550
AEAAVVGKPH EIRGEVIVAF VVLRGKLPDD QQAAEIAETL REWVSSEIGA 600
IARPEEIRFG ENLPKTRSGK LMRRLLRSLA RGETITQDIS TLENPVILEQ 650
FSQTI 655
Length:655
Mass (Da):73,338
Last modified:October 17, 2006 - v1
Checksum:iB81E66505C045F43
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000450 Genomic DNA. Translation: ABI59931.1.
RefSeqiWP_011634737.1. NC_008344.1.
YP_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:
EMBL
GenBank
DDBJ
Links Updated
CP000450 Genomic DNA. Translation: ABI59931.1 .
RefSeqi WP_011634737.1. NC_008344.1.
YP_747896.1. NC_008344.1.

3D structure databases

ProteinModelPortali Q0AFF1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 335283.Neut_1690.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABI59931 ; ABI59931 ; Neut_1690 .
GeneIDi 4273573.
KEGGi net:Neut_1690.
PATRICi 22720832. VBINitEut7577_2068.

Phylogenomic databases

eggNOGi COG0365.
HOGENOMi HOG000229981.
KOi K01895.
OMAi YNNDERF.
OrthoDBi EOG68WR2H.

Enzyme and pathway databases

BioCyci NEUT335283:GHT6-1724-MONOMER.

Family and domain databases

HAMAPi MF_01123. Ac_CoA_synth.
InterProi IPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view ]
Pfami PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR02188. Ac_CoA_lig_AcsA. 1 hit.
ProtoNeti Search...

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: September 3, 2014
This is version 57 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

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