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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp. (strain OCh 114)) (Roseobacter denitrificans)
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 sitei298Coenzyme AUniRule annotation1
Binding sitei489ATPUniRule annotation1
Binding sitei504ATPUniRule annotation1
Binding sitei512Coenzyme A; via carbonyl oxygenUniRule annotation1
Binding sitei515ATPUniRule annotation1
Metal bindingi526Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi528Magnesium; via carbonyl oxygenUniRule annotation1
Metal bindingi531Magnesium; via carbonyl oxygenUniRule annotation1
Binding sitei573Coenzyme AUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi374 – 376ATPUniRule annotation3
Nucleotide bindingi398 – 403ATPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotationImported

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 annotationImported
Ordered Locus Names:RD1_1117Imported
OrganismiRoseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp. (strain OCh 114)) (Roseobacter denitrificans)Imported
Taxonomic identifieri375451 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRoseobacter
Proteomesi
  • UP000007029 Componenti: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei598N6-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

STRINGi375451.RD1_1117.

Structurei

3D structure databases

ProteinModelPortaliQ16B70.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini12 – 69ACAS_NInterPro annotationAdd BLAST58
Domaini71 – 511AMP-bindingInterPro annotationAdd BLAST441
Domaini520 – 598AMP-binding_CInterPro annotationAdd BLAST79

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni180 – 183Coenzyme A bindingUniRule annotation4

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
KOiK01895.
OrthoDBiPOG091H059D.

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.

Q16B70-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRTPHVTLS QYASLYSESV SDSEGFWRRE GGRVDWIKPF TKVRDVNFDL
60 70 80 90 100
GSVSINWYGD GTLNVAANCV DRHLATRADQ TAIIWEPDDP KDAAKHITYK
110 120 130 140 150
QLHVSVCKMA NVLESLGVRR GDRVVIYLPM IPEAAYAMLA CARIGAIHSI
160 170 180 190 200
VFAGFSPDAL AARINGSDAK VVITADHAPR GGRATALKAN TDAALLHCKD
210 220 230 240 250
SVKCLVVKRT GGQTTWIDGR DFDCGEMMLE ASDVSHPAEM NAEDPLFILY
260 270 280 290 300
TSGSTGQPKG VVHTSGGYLT YAAMTHEIVF DYHDGDVFWC TADVGWVTGH
310 320 330 340 350
SYIVYGPLAN GATTIMFEGV PTYPDASRFW QVCEKHKVNQ FYTAPTAIRA
360 370 380 390 400
LMGQGKEFVE KCDLSDLKVL GTVGEPINPE AWNWYNDVVG KGKCPIVDTW
410 420 430 440 450
WQTETGGHLM TPLPGAHTMK PGSAMKPFFG IKPMVLEPAS GEVLEGNDVE
460 470 480 490 500
GVLVIADSWP GQMRTIWGDH ERFEKTYFSD YKGYYFTGDG CKRDADGDYW
510 520 530 540 550
ITGRVDDVIN VSGHRMGTAE VESALVAHAK VAEAAVVGYP HDIKGQGIYC
560 570 580 590 600
YVTLMNGEEP SDELYQELRK WVRAEIGPIA SPDLIQWAPG LPKTRSGKIM
610 620 630 640
RRILRKIAED DFATLGDTST LADPTVVDDL IKNRMNKQDA
Length:640
Mass (Da):70,426
Last modified:July 25, 2006 - v1
Checksum:i892116E2437F2578
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000362 Genomic DNA. Translation: ABG30773.1.
RefSeqiWP_011567395.1. NC_008209.1.

Genome annotation databases

EnsemblBacteriaiABG30773; ABG30773; RD1_1117.
KEGGirde:RD1_1117.
PATRICi23360369. VBIRosDen86677_1079.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000362 Genomic DNA. Translation: ABG30773.1.
RefSeqiWP_011567395.1. NC_008209.1.

3D structure databases

ProteinModelPortaliQ16B70.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi375451.RD1_1117.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABG30773; ABG30773; RD1_1117.
KEGGirde:RD1_1117.
PATRICi23360369. VBIRosDen86677_1079.

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
KOiK01895.
OrthoDBiPOG091H059D.

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 nameiQ16B70_ROSDO
AccessioniPrimary (citable) accession number: Q16B70
Entry historyi
Integrated into UniProtKB/TrEMBL: July 25, 2006
Last sequence update: July 25, 2006
Last modified: November 2, 2016
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference 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.