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B4SDX2 (B4SDX2_PELPB) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 37. 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 namesRecommended name:
Acetyl-coenzyme A synthetase HAMAP-Rule MF_01123

Short name=AcCoA synthetase HAMAP-Rule MF_01123
Short name=Acs HAMAP-Rule MF_01123
EC=6.2.1.1 HAMAP-Rule MF_01123
Alternative name(s):
Acetate--CoA ligase HAMAP-Rule MF_01123
Acyl-activating enzyme HAMAP-Rule MF_01123
Gene names
Name:acsA HAMAP-Rule MF_01123
Ordered Locus Names:Ppha_0664 EMBL ACF42963.1
OrganismPelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1) [Complete proteome] [HAMAP] EMBL ACF42963.1
Taxonomic identifier324925 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupPelodictyon

Protein attributes

Sequence length667 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

Region432 – 4376Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5381 By similarity HAMAP-Rule MF_01123
Metal binding5581Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5601Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5631Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3321Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3561Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site4081Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5211Substrate By similarity HAMAP-Rule MF_01123
Binding site5361Substrate By similarity HAMAP-Rule MF_01123
Binding site5441Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5471Substrate By similarity HAMAP-Rule MF_01123
Binding site6051Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6301N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
B4SDX2 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 6D0D7BD4DE17DE57

FASTA66774,643
        10         20         30         40         50         60 
MATEETTSNA QHTETSSSGE ESISSVLSEK RKFPPSAEFS NNAHISSMEE YEKLYAAAEA 

        70         80         90        100        110        120 
DPDAYWGGIA EQFHWFKKWD SVLEWNTPYA KWFNGGKTNI CYNALDVHVN SWRKNKAAII 

       130        140        150        160        170        180 
WEGEEGNQRV LTYGELHRQV SKFANVLKIA GIKPGDRVAI YMGMVPELVI AVLACARVGA 

       190        200        210        220        230        240 
VHNVIFAGFS AHAITERVND SRAKMVICAD GTRRRGGSIN LKNIVDEAIV NTPSIRSVIV 

       250        260        270        280        290        300 
LKVTDEEIHM HNGMDHWWHD LMGLAADESE PAELDAEHPL FVLYTSGSTG KPKGILHTTA 

       310        320        330        340        350        360 
GYMVHAASSF KYVFDIKDED IYFCTADVGW ITGHTYMIYG PMLNGATILM YEGAPNYPQW 

       370        380        390        400        410        420 
DRFWDIINRH KVTIFYTAPT AIRAFIRAGN EWVTKHNLSS LRLLGTVGEP INPEAWMWYQ 

       430        440        450        460        470        480 
KVVGQEKCPI VDTWWQTETG GIMVSPLPGA TPTKPGTATR PLPGIMVDVV RKDGTPCEAN 

       490        500        510        520        530        540 
EGGYLVIKKP WPSMLRTIYG DNERYEKTYW SEFHDMYFTG DGARKDEDGY IWIMGRVDDV 

       550        560        570        580        590        600 
VNVSGHRLGT SEVESALVSH EAVAEAAVVS RPDELKGNAL VAFVTLKDEY VGDMTLREAL 

       610        620        630        640        650        660 
RNHVAKEIGP IAKPDEIRWA KGLPKTRSGK IMRRLLRELA TSNEIKGDVT TLEDFGVLEN 


LRDQEND 

« Hide

References

[1]"Complete sequence of Pelodictyon phaeoclathratiforme BU-1."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 5477 / BU-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001110 Genomic DNA. Translation: ACF42963.1.
RefSeqYP_002017580.1. NC_011060.1.

3D structure databases

ProteinModelPortalB4SDX2.
SMRB4SDX2. Positions 32-665.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING324925.Ppha_0664.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF42963; ACF42963; Ppha_0664.
GeneID6461587.
KEGGpph:Ppha_0664.
PATRIC22901760. VBIPelPha134556_0672.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPPHA324925:GHBF-678-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 nameB4SDX2_PELPB
AccessionPrimary (citable) accession number: B4SDX2
Entry history
Integrated into UniProtKB/TrEMBL: September 23, 2008
Last sequence update: September 23, 2008
Last modified: February 19, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)