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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Status
Reviewed-Annotation score: 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 sitei311 – 3111Coenzyme AUniRule annotation
Binding sitei508 – 5081ATPUniRule annotation
Binding sitei523 – 5231ATPUniRule annotation
Binding sitei531 – 5311Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei534 – 5341ATPUniRule annotation
Metal bindingi545 – 5451Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi547 – 5471Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi550 – 5501Magnesium; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi387 – 3893ATPUniRule annotation
Nucleotide bindingi411 – 4166ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

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
Synonyms:acs
Ordered Locus Names:Mb3691
OrganismiMycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Taxonomic identifieri233413 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001419 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 651651Acetyl-coenzyme A synthetasePRO_0000208368Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei617 – 6171N6-acetyllysineUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Structurei

3D structure databases

ProteinModelPortaliP59871.
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

HOGENOMiHOG000229981.
KOiK01895.
OMAiDWVIYDG.
OrthoDBiEOG68WR2H.

Family and domain databases

HAMAPiMF_01123. Ac_CoA_synth.
InterProiIPR011904. Ac_CoA_lig.
IPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. 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.

P59871-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSESTPEVSS SYPPPAHFAE HANARAELYR EAEEDRLAFW AKQANRLSWT
60 70 80 90 100
TPFTEVLDWS EAPFAKWFVG GELNVAYNCV DRHVEAGHGD RVAIHWEGEP
110 120 130 140 150
VGDRRTLTYS DLLAEVSKAA NALTDLGLVA GDRVAIYLPL IPEAVIAMLA
160 170 180 190 200
CARLGIMHSV VFGGFTAAAL QARIVDAQAK LLITADGQFR RGKPSPLKAA
210 220 230 240 250
ADEALAAIPD CSVEHVLVVR RTGIEMAWSE GRDLWWHHVV GSASPAHTPE
260 270 280 290 300
PFDSEHPLFL LYTSGTTGKP KGIMHTSGGY LTQCCYTMRT IFDVKPDSDV
310 320 330 340 350
FWCTADIGWV TGHTYGVYGP LCNGVTEVLY EGTPDTPDRH RHFQIIEKYG
360 370 380 390 400
VTIYYTAPTL IRMFMKWGRE IPDSHDLSSL RLLGSVGEPI NPEAWRWYRD
410 420 430 440 450
VIGGGRTPLV DTWWQTETGS AMISPLPGIA AAKPGSAMTP LPGISAKIVD
460 470 480 490 500
DHGDPLPPHT EGAQHVTGYL VLDQPWPSML RGIWGDPARY WHSYWSKFSD
510 520 530 540 550
KGYYFAGDGA RIDPDGAIWV LGRIDDVMNV SGHRISTAEV ESALVAHSGV
560 570 580 590 600
AEAAVVGVTD ETTTQAICAF VVLRANYAPH DRTAEELRTE VARVISPIAR
610 620 630 640 650
PRDVHVVPEL PKTRSGKIMR RLLRDVAENR ELGDTSTLLD PTVFDAIRAA

K
Length:651
Mass (Da):71,548
Last modified:September 26, 2003 - v1
Checksum:i5325A7A21BB2A493
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX248333 Genomic DNA. Translation: CDO44962.1.
RefSeqiNP_857330.1. NC_002945.3.
WP_010950924.1. NC_002945.3.

Genome annotation databases

EnsemblBacteriaiCDO44962; CDO44962; Mb3691.
GeneIDi1092917.
KEGGimbo:Mb3691.
PATRICi18009832. VBIMycBov88188_4042.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX248333 Genomic DNA. Translation: CDO44962.1.
RefSeqiNP_857330.1. NC_002945.3.
WP_010950924.1. NC_002945.3.

3D structure databases

ProteinModelPortaliP59871.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCDO44962; CDO44962; Mb3691.
GeneIDi1092917.
KEGGimbo:Mb3691.
PATRICi18009832. VBIMycBov88188_4042.

Phylogenomic databases

HOGENOMiHOG000229981.
KOiK01895.
OMAiDWVIYDG.
OrthoDBiEOG68WR2H.

Family and domain databases

HAMAPiMF_01123. Ac_CoA_synth.
InterProiIPR011904. Ac_CoA_lig.
IPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. 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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-935 / AF2122/97.

Entry informationi

Entry nameiACSA_MYCBO
AccessioniPrimary (citable) accession number: P59871
Secondary accession number(s): X2BNU6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: September 26, 2003
Last modified: November 11, 2015
This is version 78 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.