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E4NDX1 (E4NDX1_KITSK) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein attributes

Sequence length651 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_01123

Catalytic activity

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. HAMAP-Rule MF_01123

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01123 SAAS SAAS011904

Post-translational modification

Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity. HAMAP-Rule MF_01123

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family. HAMAP-Rule MF_01123

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region412 – 4176Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5181 By similarity HAMAP-Rule MF_01123
Metal binding5381Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5401Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5431Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3121Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3881Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5011Substrate By similarity HAMAP-Rule MF_01123
Binding site5161Substrate By similarity HAMAP-Rule MF_01123
Binding site5241Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5271Substrate By similarity HAMAP-Rule MF_01123
Binding site5851Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6101N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
E4NDX1 [UniParc].

Last modified February 8, 2011. Version 1.
Checksum: 227EFC38369A670D

FASTA65170,350
        10         20         30         40         50         60 
MSNESLANLL KEERRFAPPA ELAASANVTA DAYAQASEDR LAFWAEQARR LSWAVEPTET 

        70         80         90        100        110        120 
LDWSNPPFAK WFADGKLNVA YNCVDRHVEA GNGDRVAIHF EGEPGDSRAI TYAQLKDEVS 

       130        140        150        160        170        180 
KAANALESLG VAKGDRVAVY LPMIPEAVVA MLACARIGAA HSVVFGGFSA DAVASRIKDA 

       190        200        210        220        230        240 
DAKLVITADG GYRRGKPSAL KPAIDEALTK VDGVENVLVV RRTGEEVAWT EGRDVWWHEL 

       250        260        270        280        290        300 
VDGQSAEHTP EAHDAEQPLF ILYTSGTTGK PKGILHTSGG YLTQASFTHN AVFDLKPETD 

       310        320        330        340        350        360 
VYWCTADIGW VTGHSYIVYG PLSNGATQVI YEGTPDTPHQ GRMFEIVQKY GVTILYTAPT 

       370        380        390        400        410        420 
LIRTWMKWGD DIPAGFDLSS LRVLGSVGEP INPEAWVWYR EHIGAGKTPI VDTWWQTETG 

       430        440        450        460        470        480 
AIMISPLPGV TETKPGSAQR ALPGIAATVV DDEAREVPNG SGGYLVLTEP WPSMLRTIWG 

       490        500        510        520        530        540 
DDERYVDTYW SRFEGRYFAG DGAKKDEDGD IWLLGRVDDV MLVSGHNIST TEVESALVGH 

       550        560        570        580        590        600 
PAVAESAVVG AADATTGQAI VAFVILRGTA ADSEELIADL RNHVGKTLGP IAKPKQIKVV 

       610        620        630        640        650 
SELPKTRSGK IMRRLLRDIA EGREVGDTTT LADSSVMNLI QSQLPAAGAE G 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP010968 Genomic DNA. Translation: BAJ29402.1.
RefSeqYP_004905358.1. NC_016109.1.

3D structure databases

ProteinModelPortalE4NDX1.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAJ29402; BAJ29402; KSE_35980.
GeneID11348269.
KEGGksk:KSE_35980.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01895.
OMAAWIWYRD.

Enzyme and pathway databases

BioCycKSET452652:GJFD-3594-MONOMER.

Family and domain databases

HAMAPMF_01123. Ac_CoA_synth.
InterProIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameE4NDX1_KITSK
AccessionPrimary (citable) accession number: E4NDX1
Entry history
Integrated into UniProtKB/TrEMBL: February 8, 2011
Last sequence update: February 8, 2011
Last modified: June 11, 2014
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)