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A1RIK1

- ACSA_SHESW

UniProt

A1RIK1 - ACSA_SHESW

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Protein
Acetyl-coenzyme A synthetase
Gene
acsA, Sputw3181_1659
Organism
Shewanella sp. (strain W3-18-1)
Status
Reviewed - Annotation score: 4 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 sitei311 – 3111Coenzyme A By similarity
Binding sitei335 – 3351Coenzyme A By similarity
Binding sitei387 – 3871Substrate; via amide nitrogen By similarity
Binding sitei500 – 5001Substrate By similarity
Binding sitei515 – 5151Substrate By similarity
Active sitei517 – 5171 By similarity
Binding sitei523 – 5231Coenzyme A By similarity
Binding sitei526 – 5261Substrate By similarity
Metal bindingi537 – 5371Magnesium; via carbonyl oxygen By similarity
Metal bindingi539 – 5391Magnesium; via carbonyl oxygen By similarity
Metal bindingi542 – 5421Magnesium; via carbonyl oxygen By similarity
Binding sitei584 – 5841Coenzyme A

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
Complete GO annotation...

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

BioCyciSSP351745:GCOY-1721-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A synthetase (EC:6.2.1.1)
Short name:
AcCoA synthetase
Short name:
Acs
Alternative name(s):
Acetate--CoA ligase
Acyl-activating enzyme
Gene namesi
Name:acsA
Ordered Locus Names:Sputw3181_1659
OrganismiShewanella sp. (strain W3-18-1)
Taxonomic identifieri351745 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
ProteomesiUP000002597: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 650650Acetyl-coenzyme A synthetaseUniRule annotation
PRO_1000065325Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei609 – 6091N6-acetyllysine By similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Interactioni

Protein-protein interaction databases

STRINGi351745.Sputw3181_1659.

Structurei

3D structure databases

ProteinModelPortaliA1RIK1.
SMRiA1RIK1. Positions 7-645.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni411 – 4166Substrate binding By similarity

Sequence similaritiesi

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.

A1RIK1-1 [UniParc]FASTAAdd to Basket

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MSSQSLYKVS GNIAANALVN NEQYKTMYQE SIVNPEGFWR EHGKRIDWIK    50
PYTKIKKTSF DDHNLSINWF YDGTLNASAN CLDRHLAEHS DRVAIIWEGD 100
NASEQRKITY GELHADVCKF ANALRSQGVR RGDIVTIYMP MVPEAAVAML 150
ACARIGAVHS VVFGGFSPDS IASRVIDGKS KVVITSDEGM RGGRAIPLKR 200
NIDDALNHPD VTSVEKVIVL KRTGGKIDWV EGRDVWWHSL LETASEHCQP 250
EEMGAEDPLF LLYTSGSTGN PKGVLHTTGG YMVYASMTHE YVFDYKAGEV 300
YWCTADVGWI TGHSYMVYGP LANGATVLIH EGVPNHPSPA RLGEMIDRHK 350
VNILYTAPTL IRALMAEGKQ HFDQFDGSTL RIMGSVGEPI NPEAWRWYHE 400
VIGHEHCPIV DTWWQTETGG ILITPLPGAT DTKPGSATRP FFGVQPALVD 450
NMGNILEGEN EGNLVLLDSW PGQMRTVYGD HERFVLTYFK TFRGMYFTGD 500
GARRDEDGYY WITGRVDDVI NVSGHRLGTA EVESALVSHE LVAEAAVVGY 550
PHDIKGQGIY AYVTLTRGTE ESEELRQELR QWVRKEIGAL ATPDLIQWAS 600
GLPKTRSGKI MRRFLRKIAA NEVTNLGDAS TLADPAVIET LIETRLNRTE 650
Length:650
Mass (Da):72,374
Last modified:February 6, 2007 - v1
Checksum:i3E623F228961B003
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000503 Genomic DNA. Translation: ABM24496.1.
RefSeqiWP_011788994.1. NC_008750.1.
YP_963050.1. NC_008750.1.

Genome annotation databases

EnsemblBacteriaiABM24496; ABM24496; Sputw3181_1659.
GeneIDi4661723.
KEGGishw:Sputw3181_1659.
PATRICi23596931. VBISheSp103602_1727.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000503 Genomic DNA. Translation: ABM24496.1 .
RefSeqi WP_011788994.1. NC_008750.1.
YP_963050.1. NC_008750.1.

3D structure databases

ProteinModelPortali A1RIK1.
SMRi A1RIK1. Positions 7-645.
ModBasei Search...

Protein-protein interaction databases

STRINGi 351745.Sputw3181_1659.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABM24496 ; ABM24496 ; Sputw3181_1659 .
GeneIDi 4661723.
KEGGi shw:Sputw3181_1659.
PATRICi 23596931. VBISheSp103602_1727.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci SSP351745:GCOY-1721-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: W3-18-1.

Entry informationi

Entry nameiACSA_SHESW
AccessioniPrimary (citable) accession number: A1RIK1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 6, 2007
Last modified: September 3, 2014
This is version 51 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

External Data

Dasty 3

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