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A1RIK1

- ACSA_SHESW

UniProt

A1RIK1 - ACSA_SHESW

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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Shewanella sp. (strain W3-18-1)
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

Mg2+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 sitei584 – 5841Coenzyme AUniRule annotation

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

BioCyciSSP351745:GCOY-1721-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: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 synthetasePRO_1000065325Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei609 – 6091N6-acetyllysineUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Interactioni

Protein-protein interaction databases

STRINGi351745.Sputw3181_1659.

Structurei

3D structure databases

ProteinModelPortaliA1RIK1.
SMRiA1RIK1. Positions 7-645.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni191 – 1944Coenzyme 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.

A1RIK1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSQSLYKVS GNIAANALVN NEQYKTMYQE SIVNPEGFWR EHGKRIDWIK
60 70 80 90 100
PYTKIKKTSF DDHNLSINWF YDGTLNASAN CLDRHLAEHS DRVAIIWEGD
110 120 130 140 150
NASEQRKITY GELHADVCKF ANALRSQGVR RGDIVTIYMP MVPEAAVAML
160 170 180 190 200
ACARIGAVHS VVFGGFSPDS IASRVIDGKS KVVITSDEGM RGGRAIPLKR
210 220 230 240 250
NIDDALNHPD VTSVEKVIVL KRTGGKIDWV EGRDVWWHSL LETASEHCQP
260 270 280 290 300
EEMGAEDPLF LLYTSGSTGN PKGVLHTTGG YMVYASMTHE YVFDYKAGEV
310 320 330 340 350
YWCTADVGWI TGHSYMVYGP LANGATVLIH EGVPNHPSPA RLGEMIDRHK
360 370 380 390 400
VNILYTAPTL IRALMAEGKQ HFDQFDGSTL RIMGSVGEPI NPEAWRWYHE
410 420 430 440 450
VIGHEHCPIV DTWWQTETGG ILITPLPGAT DTKPGSATRP FFGVQPALVD
460 470 480 490 500
NMGNILEGEN EGNLVLLDSW PGQMRTVYGD HERFVLTYFK TFRGMYFTGD
510 520 530 540 550
GARRDEDGYY WITGRVDDVI NVSGHRLGTA EVESALVSHE LVAEAAVVGY
560 570 580 590 600
PHDIKGQGIY AYVTLTRGTE ESEELRQELR QWVRKEIGAL ATPDLIQWAS
610 620 630 640 650
GLPKTRSGKI MRRFLRKIAA NEVTNLGDAS TLADPAVIET LIETRLNRTE
Length:650
Mass (Da):72,374
Last modified:February 6, 2007 - v1
Checksum:i3E623F228961B003
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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...
MobiDBi 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: November 26, 2014
This is version 53 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