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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Pseudomonas mendocina (strain NK-01)
Status
Unreviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei311Coenzyme AUniRule annotation1
Binding sitei335Coenzyme AUniRule annotation1
Binding sitei500ATPUniRule annotation1
Binding sitei515ATPUniRule annotation1
Binding sitei523Coenzyme A; via carbonyl oxygenUniRule annotation1
Binding sitei526ATPUniRule annotation1
Metal bindingi537Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi539Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi542Magnesium; via carbonyl oxygenUniRule annotation1
Binding sitei584Coenzyme AUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi387 – 389ATPUniRule annotation3
Nucleotide bindingi411 – 416ATPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotation

Keywords - Ligandi

ATP-bindingUniRule annotation, MagnesiumUniRule annotation, Metal-bindingUniRule annotation, Nucleotide-binding

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:MDS_3395Imported
OrganismiPseudomonas mendocina (strain NK-01)Imported
Taxonomic identifieri1001585 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000008306 Componenti: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei609N6-acetyllysineUniRule annotation1

Post-translational modificationi

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

Keywords - PTMi

AcetylationUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi1001585.MDS_3395.

Structurei

3D structure databases

ProteinModelPortaliF4DQJ9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – 81ACAS_NInterPro annotationAdd BLAST58
Domaini83 – 522AMP-bindingInterPro annotationAdd BLAST440
Domaini531 – 609AMP-binding_CInterPro annotationAdd BLAST79

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni191 – 194Coenzyme A bindingUniRule annotation4

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
KOiK01895.
OMAiGPLANGC.

Family and domain databases

CDDicd05966. ACS. 1 hit.
HAMAPiMF_01123. Ac_CoA_synth. 1 hit.
InterProiIPR011904. Ac_CoA_lig.
IPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. 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.

F4DQJ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAASLYPVR PEVAARTLTD EATYKAMYQQ SVVNPEGFWR EQGKRIDWIK
60 70 80 90 100
PYTKVKQTTF DDHHVDIKWY ADGTLNVSYN CLDRHLEERG DQVAIIWEGD
110 120 130 140 150
DPSEHREITY RQLHEEVSKF ANALRGQDVH RGDVVTIYMP MIPEAVVAML
160 170 180 190 200
ACARIGAIHS VVFGGFSPEA LAGRIIDCES KVVITADEGL RGGRKVPLKA
210 220 230 240 250
NVDDALTNPE TASVQKIIVV KRTGSDIKWN QHRDIWYEDL MKVAGSVCAP
260 270 280 290 300
KEMGAEEALF ILYTSGSTGK PKGVLHTTGG YLTYASLTHE RVFDYRPGEV
310 320 330 340 350
FWCTADIGWV TGHTYLVYGP LSNGATTLMF EGVPNYPDVR RVAQIVDKHK
360 370 380 390 400
VNILYTAPTA IRAMMAEGKA AVEGADGSSL RLLGSVGEPI NPEAWQWYYE
410 420 430 440 450
NVGQSRCPIV DTWWQTETGA CLMTPLPGAH GLKPGSAARP FFGVQPALVD
460 470 480 490 500
NLGNIIEGPA EGNLVIIDSW PGQARTLYGD HDRFVDTYFK TFRGMYFTGD
510 520 530 540 550
GARRDEDGYW WITGRVDDVL NVSGHRMGTA EVESAMVAHP KVAEAAVVGV
560 570 580 590 600
PHDIKGQGIY VYVTLNAGEE SSEQLRQELK NWVRKEIGPI ATPDVIQWAP
610 620 630 640 650
GLPKTRSGKI MRRILRKIAT AEYDSLGDIS TLADPGVVQH LIDTHRQMQA

ACA
Length:653
Mass (Da):72,265
Last modified:June 28, 2011 - v1
Checksum:iFAD6AE26483A4D3D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002620 Genomic DNA. Translation: AEB59426.1.
RefSeqiWP_003462147.1. NC_015410.1.

Genome annotation databases

EnsemblBacteriaiAEB59426; AEB59426; MDS_3395.
KEGGipmk:MDS_3395.
PATRICi54487546. VBIPseMen187712_3448.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002620 Genomic DNA. Translation: AEB59426.1.
RefSeqiWP_003462147.1. NC_015410.1.

3D structure databases

ProteinModelPortaliF4DQJ9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi1001585.MDS_3395.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAEB59426; AEB59426; MDS_3395.
KEGGipmk:MDS_3395.
PATRICi54487546. VBIPseMen187712_3448.

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
KOiK01895.
OMAiGPLANGC.

Family and domain databases

CDDicd05966. ACS. 1 hit.
HAMAPiMF_01123. Ac_CoA_synth. 1 hit.
InterProiIPR011904. Ac_CoA_lig.
IPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiF4DQJ9_PSEMN
AccessioniPrimary (citable) accession number: F4DQJ9
Entry historyi
Integrated into UniProtKB/TrEMBL: June 28, 2011
Last sequence update: June 28, 2011
Last modified: November 2, 2016
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.