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Q98ET8

- ACSA_RHILO

UniProt

Q98ET8 - ACSA_RHILO

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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Rhizobium loti (strain MAFF303099) (Mesorhizobium loti)
Status
Reviewed - 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 sitei312 – 3121Coenzyme AUniRule annotation
Binding sitei336 – 3361Coenzyme AUniRule annotation
Binding sitei501 – 5011ATPUniRule annotation
Binding sitei516 – 5161ATPUniRule annotation
Binding sitei524 – 5241Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei527 – 5271ATPUniRule annotation
Metal bindingi538 – 5381Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi540 – 5401Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi543 – 5431Magnesium; via carbonyl oxygenUniRule annotation
Binding sitei585 – 5851Coenzyme AUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi388 – 3903ATPUniRule annotation
Nucleotide bindingi412 – 4176ATPUniRule 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

BioCyciMLOT266835:GJ9L-3186-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: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 synthetasePRO_0000208380Add
BLAST

Amino acid modifications

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

STRINGi266835.mlr4089.

Structurei

3D structure databases

ProteinModelPortaliQ98ET8.
SMRiQ98ET8. Positions 5-647.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni190 – 1934Coenzyme A bindingUniRule annotation

Sequence similaritiesi

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

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

        10         20         30         40         50
MSEVHVHRVQ PAWKKNALID NDTYLKWYAD SIKNPDKFWG KHGKRIDWFK
60 70 80 90 100
PFSKVKNTSF DGKVSIKWFE DGLTNVSYNC IDRHLKKRGD QTAIIWEGDN
110 120 130 140 150
PYDDKKITYN ELYERVCRLA NVMKKHGVKK GDRVTIYMPM IPEAAYAMLA
160 170 180 190 200
CTRIGAIHSI VFGGFSPDAL AGRIVDCEST FVITADEGLR GGKSIPLKEN
210 220 230 240 250
TDKAIDIAAK NFVMVKNVLV VRRTGGKVGW APGRDLWYHD EVATVKAECK
260 270 280 290 300
PEKMKAEDPL FILYTSGSTG KPKGVLHTTA GYLVYASMTH QYVFDYHDGD
310 320 330 340 350
IYWCTADVGW VTGHSYIVYG PLANGATTLM FEGVPNYPSQ SRFWEVIDKH
360 370 380 390 400
KVNIFYTAPT ALRALMGAGN DPVKKTSRKS LRVLGSVGEP INPEAWEWYF
410 420 430 440 450
NVVGNGKVPI VDTWWQTETG GILITPLPGA TDLKAGSATR PFFGVKPQLV
460 470 480 490 500
DGEGKVLEGA ADGNLCITDS WPGQMRTVYG DHDRFVQTYF STYKGKYFTG
510 520 530 540 550
DGCRRDADGY YWITGRVDDV INVSGHRMGT AEVESALVSH DKVSEAAVVG
560 570 580 590 600
YPHDIKGQGI YSYVTLMKGE EPTEDLRKEL IAHVRKEIGA IASPDKIQFA
610 620 630 640 650
PGLPKTRSGK IMRRILRKIA EDDFSTLGDT STLADPAVVD DLIANRQNKK

G
Length:651
Mass (Da):72,530
Last modified:October 1, 2001 - v1
Checksum:iC7A0AC5011C4D43F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: November 26, 2014
This is version 72 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

External Data

Dasty 3