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Q88EH6

- ACSA1_PSEPK

UniProt

Q88EH6 - ACSA1_PSEPK

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Protein
Acetyl-coenzyme A synthetase 1
Gene
acsA1, PP_4487
Organism
Pseudomonas putida (strain KT2440)
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

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

BioCyciPPUT160488:GIXO-4574-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A synthetase 1 (EC:6.2.1.1)
Short name:
AcCoA synthetase 1
Short name:
Acs 1
Alternative name(s):
Acetate--CoA ligase 1
Acyl-activating enzyme 1
Gene namesi
Name:acsA1
Ordered Locus Names:PP_4487
OrganismiPseudomonas putida (strain KT2440)
Taxonomic identifieri160488 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000000556: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 653653Acetyl-coenzyme A synthetase 1UniRule annotation
PRO_0000208376Add
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

STRINGi160488.PP_4487.

Structurei

3D structure databases

ProteinModelPortaliQ88EH6.
SMRiQ88EH6. Positions 7-647.

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiGGCEAVT.
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.

Q88EH6-1 [UniParc]FASTAAdd to Basket

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MSAAPLYPVR PEVAATTLTD EATYKAMYQQ SVINPDGFWR EQAQRIDWIK    50
PFTKVKQTSF DDHHVDIKWF ADGTLNVSSN CLDRHLEERG DQLAIIWEGD 100
DPSEHRNITY RELHEQVCKF ANALRGQDVH RGDVVTIYMP MIPEAVVAML 150
ACARIGAIHS VVFGGFSPEA LAGRIIDCKS KVVITADEGV RGGRRTPLKA 200
NVDLALTNPE TSSVQKIIVC KRTGGDIAWH QHRDIWYEDL MKVASSHCAP 250
KEMGAEEALF ILYTSGSTGK PKGVLHTTGG YLVYAALTHE RVFDYRPGEV 300
YWCTADVGWV TGHSYIVYGP LANGATTLLF EGVPNYPDIT RVSKIVDKHK 350
VNILYTAPTA IRAMMAEGQA AVEGADGSSL RLLGSVGEPI NPEAWNWYYK 400
TVGKERCPIV DTWWQTETGG ILISPLPGAT GLKPGSATRP FFGVVPALVD 450
NLGNLIDGAA EGNLVILDSW PGQSRSLYGD HDRFVDTYFK TFRGMYFTGD 500
GARRDEDGYY WITGRVDDVL NVSGHRMGTA EIESAMVAHS KVAEAAVVGV 550
PHDIKGQGIY VYVTLNAGIE ASEQLRLELK NWVRKEIGPI ASPDVIQWAP 600
GLPKTRSGKI MRRILRKIAT GEYDALGDIS TLADPGVVQH LIDTHKAMNL 650
ASA 653
Length:653
Mass (Da):71,797
Last modified:June 1, 2003 - v1
Checksum:iCE626C86C922E8F4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE015451 Genomic DNA. Translation: AAN70062.1.
RefSeqiNP_746598.1. NC_002947.3.

Genome annotation databases

EnsemblBacteriaiAAN70062; AAN70062; PP_4487.
GeneIDi1042436.
KEGGippu:PP_4487.
PATRICi19947676. VBIPsePut30601_4775.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE015451 Genomic DNA. Translation: AAN70062.1 .
RefSeqi NP_746598.1. NC_002947.3.

3D structure databases

ProteinModelPortali Q88EH6.
SMRi Q88EH6. Positions 7-647.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 160488.PP_4487.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAN70062 ; AAN70062 ; PP_4487 .
GeneIDi 1042436.
KEGGi ppu:PP_4487.
PATRICi 19947676. VBIPsePut30601_4775.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci PPUT160488:GIXO-4574-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: KT2440.

Entry informationi

Entry nameiACSA1_PSEPK
AccessioniPrimary (citable) accession number: Q88EH6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 69 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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