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Q2YLH5

- ACSA_BRUA2

UniProt

Q2YLH5 - ACSA_BRUA2

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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Brucella abortus (strain 2308)
Status
Reviewed - 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

Magnesium.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei311 – 3111Coenzyme AUniRule annotation
Binding sitei335 – 3351Coenzyme AUniRule annotation
Binding sitei500 – 5001ATPUniRule annotation
Binding sitei515 – 5151ATPUniRule annotation
Binding sitei523 – 5231Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei526 – 5261ATPUniRule annotation
Metal bindingi537 – 5371Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi539 – 5391Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi542 – 5421Magnesium; via carbonyl oxygenUniRule annotation
Binding sitei586 – 5861Coenzyme A

Regions

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

GO - Molecular functioni

  1. acetate-CoA ligase activity Source: UniProtKB-HAMAP
  2. AMP binding Source: InterPro
  3. ATP binding Source: UniProtKB-KW
  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

Ligase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciBABO359391:GKDV-1863-MONOMER.
BMEL359391:GJOQ-1863-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 ligaseUniRule annotation
Acyl-activating enzymeUniRule annotation
Gene namesi
Name:acsAUniRule annotation
Ordered Locus Names:BAB1_1819
OrganismiBrucella abortus (strain 2308)
Taxonomic identifieri359391 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
ProteomesiUP000002719: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 651651Acetyl-coenzyme A synthetasePRO_1000065274Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei611 – 6111N6-acetyllysineUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiQ2YLH5.

Interactioni

Protein-protein interaction databases

STRINGi359391.BAB1_1819.

Structurei

3D structure databases

ProteinModelPortaliQ2YLH5.
SMRiQ2YLH5. Positions 17-648.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni189 – 1924Coenzyme A bindingUniRule annotation

Sequence similaritiesi

Belongs to the ATP-dependent AMP-binding enzyme family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiAWIWYRD.
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.

Q2YLH5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSEKLYPVLP EAKKNTLIDN ETYLEWYEES VSDPDGFWAK HGRRIDWFKP
60 70 80 90 100
FTKVKNTDFN GDVTIKWYED GVTNVSYNCI DRHLKSRGDK VAIIWEGDNP
110 120 130 140 150
YIDKKITYRE LYENVCRMAN VLKKHGVKKG DRVTIYLPMI PEAAYAMLAC
160 170 180 190 200
ARIGAVHSVV FAGFSPEALA GRIVDCESTF VITADEGVRG GKPVALKENT
210 220 230 240 250
DTAIDIAAKQ YVMVNKVLVV RRTGGKVSWG RGRDLWYHQE VASVEPHCEP
260 270 280 290 300
EPMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYASMTHQ YVFDYHDGEI
310 320 330 340 350
YWCTADVGWV TGHSYIVYGP LANGATTLMF EGVPNFPDQG RFWEVVDKHH
360 370 380 390 400
VNIFYTAPTA LRALMGAGDE FVTRSSRSTL RLLGSVGEPI NPEAWEWYYN
410 420 430 440 450
VVGDQKCPIV DTWWQTENGG ILITPLPGAT DLKPGSATRP FFGVKPVLVD
460 470 480 490 500
NEGNVQEGVA DGNLCISDSW PGQMRTVYGD HKRFIETYFS TYKGMYFSGD
510 520 530 540 550
GCRRDEDGYY WITGRVDDVL NISGHRLGTA EIESALVSHH SVSEAAVVGY
560 570 580 590 600
PHPIKGQGIY CYVTLMTGAD AQDPDELRKE LVQHVRKEIG PIATPDKIQF
610 620 630 640 650
APGLPKTRSG KIMRRILRKI AEDEFGALGD TSTLADPGVV DDLIENRQNK

K
Length:651
Mass (Da):72,731
Last modified:February 7, 2006 - v1
Checksum:i7FB222A3EE6476CE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM040264 Genomic DNA. Translation: CAJ11775.1.
RefSeqiYP_415165.1. NC_007618.1.

Genome annotation databases

EnsemblBacteriaiCAJ11775; CAJ11775; BAB1_1819.
GeneIDi3788319.
KEGGibmf:BAB1_1819.
PATRICi17846672. VBIBruMel86222_1885.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM040264 Genomic DNA. Translation: CAJ11775.1 .
RefSeqi YP_415165.1. NC_007618.1.

3D structure databases

ProteinModelPortali Q2YLH5.
SMRi Q2YLH5. Positions 17-648.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 359391.BAB1_1819.

Proteomic databases

PRIDEi Q2YLH5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAJ11775 ; CAJ11775 ; BAB1_1819 .
GeneIDi 3788319.
KEGGi bmf:BAB1_1819.
PATRICi 17846672. VBIBruMel86222_1885.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci BABO359391:GKDV-1863-MONOMER.
BMEL359391:GJOQ-1863-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 2308.

Entry informationi

Entry nameiACSA_BRUA2
AccessioniPrimary (citable) accession number: Q2YLH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 7, 2006
Last modified: October 1, 2014
This is version 52 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, Reference proteome

Documents

  1. Brucella abortus strain 2308
    Brucella abortus (strain 2308): entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3