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B4EEM3 (B4EEM3_BURCJ) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length660 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

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

Region421 – 4266Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5301 By similarity HAMAP-Rule MF_01123
Metal binding5501Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5521Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5551Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3171Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3971Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5121Substrate By similarity HAMAP-Rule MF_01123
Binding site5281Substrate By similarity HAMAP-Rule MF_01123
Binding site5361Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5391Substrate By similarity HAMAP-Rule MF_01123
Binding site6001Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6251N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
B4EEM3 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 1D3EA6C06B20F342

FASTA66072,326
        10         20         30         40         50         60 
MSAIESVLHE TRQFAPPAAL EKTAAISGMP AYRALVAEAE QDYEGFWARL AREGLTWHKP 

        70         80         90        100        110        120 
FTKVLDERNA PFYTWFDDGE LNASYNCLDR HVEAGHGERV AVIFEADDGT VTRVTYADLL 

       130        140        150        160        170        180 
ARVSRFANAL KKRGIGKGDR VVIYIPMSIE GIVAMQACAR IGATHSVVFG GFSAKSLNER 

       190        200        210        220        230        240 
LVDVGAVALI TADEQARGGK TLPLKSIADE AIALGGCEAV KSVIVYRRTG GKIDWHADRD 

       250        260        270        280        290        300 
LWMHELVDGE SDRCEPTWVG AEHPLFILYT SGSTGKPKGV QHSTGGYLLW AAQTMKWTFD 

       310        320        330        340        350        360 
WKPDDVFWCT ADIGWVTGHT YITYGPLACG GTQVVFEGVP TYPDAGRFWK MIGDHKVTVF 

       370        380        390        400        410        420 
YTAPTAIRSL IKAAEADDKV HPKSYDLSSL RIIGTVGEPI NPEAWMWYHK HVGHERCPIV 

       430        440        450        460        470        480 
DTWWQTETGG HMITPLPGAT PTVPGSCTLP LPGITAAVVD ETGQDVPNGQ GGILVVKRPW 

       490        500        510        520        530        540 
PAMIRTIWGD PERFKKSYYP EELGGTLYLA GDGTVRDKET GYFTIMGRID DVLNVSGHRL 

       550        560        570        580        590        600 
GTMEIESALV SHELVAEAAV VGRPDDTTGE AVVAFVVLKR SRPEGDEAAA LAKTLRDWVG 

       610        620        630        640        650        660 
KQIGPIAKPK DIRFGDNLPK TRSGKIMRRL LRSLAKGEAI TQDTSTLENP AILEQLTEVR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM747720 Genomic DNA. Translation: CAR52585.1.
RefSeqYP_002231409.1. NC_011000.1.

3D structure databases

ProteinModelPortalB4EEM3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING216591.BCAL2284.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6932391.
KEGGbcj:BCAL2284.
PATRIC19076480. VBIBurCen118154_2384.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAWVMGRVD.
OrthoDBEOG68WR2H.
ProtClustDBPRK00174.

Enzyme and pathway databases

BioCycBCEN216591:GJI4-2332-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 nameB4EEM3_BURCJ
AccessionPrimary (citable) accession number: B4EEM3
Entry history
Integrated into UniProtKB/TrEMBL: September 23, 2008
Last sequence update: September 23, 2008
Last modified: February 19, 2014
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)