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Q88EH6

- ACSA1_PSEPK

UniProt

Q88EH6 - ACSA1_PSEPK

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Protein

Acetyl-coenzyme A synthetase 1

Gene

acsA1

Organism
Pseudomonas putida (strain KT2440)
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 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

BioCyciPPUT160488:GIXO-4574-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A synthetase 1UniRule annotation (EC:6.2.1.1UniRule annotation)
Short name:
AcCoA synthetase 1UniRule annotation
Short name:
Acs 1UniRule annotation
Alternative name(s):
Acetate--CoA ligase 1UniRule annotation
Acyl-activating enzyme 1UniRule annotation
Gene namesi
Name:acsA1UniRule annotation
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 1PRO_0000208376Add
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

STRINGi160488.PP_4487.

Structurei

3D structure databases

ProteinModelPortaliQ88EH6.
SMRiQ88EH6. Positions 7-647.
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.
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

« Hide

        10         20         30         40         50
MSAAPLYPVR PEVAATTLTD EATYKAMYQQ SVINPDGFWR EQAQRIDWIK
60 70 80 90 100
PFTKVKQTSF DDHHVDIKWF ADGTLNVSSN CLDRHLEERG DQLAIIWEGD
110 120 130 140 150
DPSEHRNITY RELHEQVCKF ANALRGQDVH RGDVVTIYMP MIPEAVVAML
160 170 180 190 200
ACARIGAIHS VVFGGFSPEA LAGRIIDCKS KVVITADEGV RGGRRTPLKA
210 220 230 240 250
NVDLALTNPE TSSVQKIIVC KRTGGDIAWH QHRDIWYEDL MKVASSHCAP
260 270 280 290 300
KEMGAEEALF ILYTSGSTGK PKGVLHTTGG YLVYAALTHE RVFDYRPGEV
310 320 330 340 350
YWCTADVGWV TGHSYIVYGP LANGATTLLF EGVPNYPDIT RVSKIVDKHK
360 370 380 390 400
VNILYTAPTA IRAMMAEGQA AVEGADGSSL RLLGSVGEPI NPEAWNWYYK
410 420 430 440 450
TVGKERCPIV DTWWQTETGG ILISPLPGAT GLKPGSATRP FFGVVPALVD
460 470 480 490 500
NLGNLIDGAA EGNLVILDSW PGQSRSLYGD HDRFVDTYFK TFRGMYFTGD
510 520 530 540 550
GARRDEDGYY WITGRVDDVL NVSGHRMGTA EIESAMVAHS KVAEAAVVGV
560 570 580 590 600
PHDIKGQGIY VYVTLNAGIE ASEQLRLELK NWVRKEIGPI ASPDVIQWAP
610 620 630 640 650
GLPKTRSGKI MRRILRKIAT GEYDALGDIS TLADPGVVQH LIDTHKAMNL

ASA
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: October 1, 2014
This is version 70 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3