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B4SDX2

- B4SDX2_PELPB

UniProt

B4SDX2 - B4SDX2_PELPB

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Protein
Acetyl-coenzyme A synthetase
Gene
acsA, Ppha_0664
Organism
Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1)
Status
Unreviewed - 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 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 sitei332 – 3321Coenzyme A By similarityUniRule annotation
Binding sitei356 – 3561Coenzyme A By similarityUniRule annotation
Binding sitei408 – 4081Substrate; via nitrogen amide By similarityUniRule annotation
Binding sitei521 – 5211Substrate By similarityUniRule annotation
Binding sitei536 – 5361Substrate By similarityUniRule annotation
Active sitei538 – 5381 By similarityUniRule annotation
Binding sitei544 – 5441Coenzyme A By similarityUniRule annotation
Binding sitei547 – 5471Substrate By similarityUniRule annotation
Metal bindingi558 – 5581Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi560 – 5601Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi563 – 5631Magnesium; via carbonyl oxygen By similarityUniRule annotation
Binding sitei605 – 6051Coenzyme A By similarityUniRule annotation

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

LigaseUniRule annotationImported

Keywords - Ligandi

ATP-bindingUniRule annotation, MagnesiumUniRule annotation, Metal-bindingUniRule annotation, Nucleotide-binding

Enzyme and pathway databases

BioCyciPPHA324925:GHBF-678-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 ligase
Acyl-activating enzyme
Gene namesi
Name:acsAUniRule annotation
Ordered Locus Names:Ppha_0664Imported
OrganismiPelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1)Imported
Taxonomic identifieri324925 [NCBI]
Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupPelodictyon
ProteomesiUP000002724: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei630 – 6301N6-acetyllysine By similarityUniRule annotation

Post-translational modificationi

Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity.UniRule annotation

Keywords - PTMi

AcetylationUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi324925.Ppha_0664.

Structurei

3D structure databases

ProteinModelPortaliB4SDX2.
SMRiB4SDX2. Positions 32-665.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni432 – 4376Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiVEWMDSE.
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.

B4SDX2-1 [UniParc]FASTAAdd to Basket

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MATEETTSNA QHTETSSSGE ESISSVLSEK RKFPPSAEFS NNAHISSMEE    50
YEKLYAAAEA DPDAYWGGIA EQFHWFKKWD SVLEWNTPYA KWFNGGKTNI 100
CYNALDVHVN SWRKNKAAII WEGEEGNQRV LTYGELHRQV SKFANVLKIA 150
GIKPGDRVAI YMGMVPELVI AVLACARVGA VHNVIFAGFS AHAITERVND 200
SRAKMVICAD GTRRRGGSIN LKNIVDEAIV NTPSIRSVIV LKVTDEEIHM 250
HNGMDHWWHD LMGLAADESE PAELDAEHPL FVLYTSGSTG KPKGILHTTA 300
GYMVHAASSF KYVFDIKDED IYFCTADVGW ITGHTYMIYG PMLNGATILM 350
YEGAPNYPQW DRFWDIINRH KVTIFYTAPT AIRAFIRAGN EWVTKHNLSS 400
LRLLGTVGEP INPEAWMWYQ KVVGQEKCPI VDTWWQTETG GIMVSPLPGA 450
TPTKPGTATR PLPGIMVDVV RKDGTPCEAN EGGYLVIKKP WPSMLRTIYG 500
DNERYEKTYW SEFHDMYFTG DGARKDEDGY IWIMGRVDDV VNVSGHRLGT 550
SEVESALVSH EAVAEAAVVS RPDELKGNAL VAFVTLKDEY VGDMTLREAL 600
RNHVAKEIGP IAKPDEIRWA KGLPKTRSGK IMRRLLRELA TSNEIKGDVT 650
TLEDFGVLEN LRDQEND 667
Length:667
Mass (Da):74,643
Last modified:September 23, 2008 - v1
Checksum:i6D0D7BD4DE17DE57
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001110 Genomic DNA. Translation: ACF42963.1.
RefSeqiWP_012507458.1. NC_011060.1.
YP_002017580.1. NC_011060.1.

Genome annotation databases

EnsemblBacteriaiACF42963; ACF42963; Ppha_0664.
GeneIDi6461587.
KEGGipph:Ppha_0664.
PATRICi22901760. VBIPelPha134556_0672.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001110 Genomic DNA. Translation: ACF42963.1 .
RefSeqi WP_012507458.1. NC_011060.1.
YP_002017580.1. NC_011060.1.

3D structure databases

ProteinModelPortali B4SDX2.
SMRi B4SDX2. Positions 32-665.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 324925.Ppha_0664.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACF42963 ; ACF42963 ; Ppha_0664 .
GeneIDi 6461587.
KEGGi pph:Ppha_0664.
PATRICi 22901760. VBIPelPha134556_0672.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci PPHA324925:GHBF-678-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. "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.
    , 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.

Entry informationi

Entry nameiB4SDX2_PELPB
AccessioniPrimary (citable) accession number: B4SDX2
Entry historyi
Integrated into UniProtKB/TrEMBL: September 23, 2008
Last sequence update: September 23, 2008
Last modified: September 3, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

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