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Q98ET8

- ACSA_RHILO

UniProt

Q98ET8 - ACSA_RHILO

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Protein
Acetyl-coenzyme A synthetase
Gene
acsA, mlr4089
Organism
Rhizobium loti (strain MAFF303099) (Mesorhizobium loti)
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 sitei312 – 3121Coenzyme A By similarity
Binding sitei336 – 3361Coenzyme A By similarity
Binding sitei388 – 3881Substrate; via amide nitrogen By similarity
Binding sitei501 – 5011Substrate By similarity
Binding sitei516 – 5161Substrate By similarity
Active sitei518 – 5181 By similarity
Binding sitei524 – 5241Coenzyme A By similarity
Binding sitei527 – 5271Substrate By similarity
Metal bindingi538 – 5381Magnesium; via carbonyl oxygen By similarity
Metal bindingi540 – 5401Magnesium; via carbonyl oxygen By similarity
Metal bindingi543 – 5431Magnesium; via carbonyl oxygen By similarity
Binding sitei585 – 5851Coenzyme 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

BioCyciMLOT266835:GJ9L-3186-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:mlr4089
OrganismiRhizobium loti (strain MAFF303099) (Mesorhizobium loti)
Taxonomic identifieri266835 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium
ProteomesiUP000000552: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 651651Acetyl-coenzyme A synthetaseUniRule annotation
PRO_0000208380Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei610 – 6101N6-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

STRINGi266835.mlr4089.

Structurei

3D structure databases

ProteinModelPortaliQ98ET8.
SMRiQ98ET8. Positions 5-647.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni412 – 4176Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiQTAILFE.
OrthoDBiEOG68WR2H.

Family and domain databases

HAMAPiMF_01123. Ac_CoA_synth.
InterProiIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
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.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q98ET8-1 [UniParc]FASTAAdd to Basket

« Hide

MSEVHVHRVQ PAWKKNALID NDTYLKWYAD SIKNPDKFWG KHGKRIDWFK    50
PFSKVKNTSF DGKVSIKWFE DGLTNVSYNC IDRHLKKRGD QTAIIWEGDN 100
PYDDKKITYN ELYERVCRLA NVMKKHGVKK GDRVTIYMPM IPEAAYAMLA 150
CTRIGAIHSI VFGGFSPDAL AGRIVDCEST FVITADEGLR GGKSIPLKEN 200
TDKAIDIAAK NFVMVKNVLV VRRTGGKVGW APGRDLWYHD EVATVKAECK 250
PEKMKAEDPL FILYTSGSTG KPKGVLHTTA GYLVYASMTH QYVFDYHDGD 300
IYWCTADVGW VTGHSYIVYG PLANGATTLM FEGVPNYPSQ SRFWEVIDKH 350
KVNIFYTAPT ALRALMGAGN DPVKKTSRKS LRVLGSVGEP INPEAWEWYF 400
NVVGNGKVPI VDTWWQTETG GILITPLPGA TDLKAGSATR PFFGVKPQLV 450
DGEGKVLEGA ADGNLCITDS WPGQMRTVYG DHDRFVQTYF STYKGKYFTG 500
DGCRRDADGY YWITGRVDDV INVSGHRMGT AEVESALVSH DKVSEAAVVG 550
YPHDIKGQGI YSYVTLMKGE EPTEDLRKEL IAHVRKEIGA IASPDKIQFA 600
PGLPKTRSGK IMRRILRKIA EDDFSTLGDT STLADPAVVD DLIANRQNKK 650
G 651
Length:651
Mass (Da):72,530
Last modified:October 1, 2001 - v1
Checksum:iC7A0AC5011C4D43F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000012 Genomic DNA. Translation: BAB50829.1.
RefSeqiNP_105043.1. NC_002678.2.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000012 Genomic DNA. Translation: BAB50829.1 .
RefSeqi NP_105043.1. NC_002678.2.

3D structure databases

ProteinModelPortali Q98ET8.
SMRi Q98ET8. Positions 5-647.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 266835.mlr4089.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB50829 ; BAB50829 ; BAB50829 .
GeneIDi 1227704.
KEGGi mlo:mlr4089.
PATRICi 22480693. VBIMesLot2464_3234.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci MLOT266835:GJ9L-3186-MONOMER.

Family and domain databases

HAMAPi MF_01123. Ac_CoA_synth.
InterProi IPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
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.
PROSITEi PS00455. AMP_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MAFF303099.

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: May 14, 2014
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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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