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Q16B70

- Q16B70_ROSDO

UniProt

Q16B70 - Q16B70_ROSDO

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Protein

Acetyl-coenzyme A synthetase

Gene
acsA, RD1_1117
Organism
Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp. (strain OCh 114)) (Roseobacter denitrificans)
Status
Unreviewed - 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 By similarity.UniRule annotation

Catalytic activityi

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.UniRule annotation

Cofactori

Magnesium By similarity.UniRule annotationSAAS annotations

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei298 – 2981Coenzyme A By similarityUniRule annotation
Binding sitei374 – 3741Substrate; via nitrogen amide By similarityUniRule annotation
Binding sitei489 – 4891Substrate By similarityUniRule annotation
Binding sitei504 – 5041Substrate By similarityUniRule annotation
Active sitei506 – 5061 By similarityUniRule annotation
Binding sitei512 – 5121Coenzyme A By similarityUniRule annotation
Binding sitei515 – 5151Substrate By similarityUniRule annotation
Metal bindingi526 – 5261Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi528 – 5281Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi531 – 5311Magnesium; via carbonyl oxygen By similarityUniRule annotation
Binding sitei573 – 5731Coenzyme A By similarityUniRule 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

LigaseUniRule annotationImported

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciRDEN375451:GJIZ-1047-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 ligase
Acyl-activating enzyme
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
ProteomesiUP000007029: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei598 – 5981N6-acetyllysine By similarityUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

AcetylationUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi375451.RD1_1117.

Structurei

3D structure databases

ProteinModelPortaliQ16B70.
SMRiQ16B70. Positions 11-634.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni398 – 4036Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
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.

Q16B70-1 [UniParc]FASTAAdd to Basket

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MTRTPHVTLS QYASLYSESV SDSEGFWRRE GGRVDWIKPF TKVRDVNFDL    50
GSVSINWYGD GTLNVAANCV DRHLATRADQ TAIIWEPDDP KDAAKHITYK 100
QLHVSVCKMA NVLESLGVRR GDRVVIYLPM IPEAAYAMLA CARIGAIHSI 150
VFAGFSPDAL AARINGSDAK VVITADHAPR GGRATALKAN TDAALLHCKD 200
SVKCLVVKRT GGQTTWIDGR DFDCGEMMLE ASDVSHPAEM NAEDPLFILY 250
TSGSTGQPKG VVHTSGGYLT YAAMTHEIVF DYHDGDVFWC TADVGWVTGH 300
SYIVYGPLAN GATTIMFEGV PTYPDASRFW QVCEKHKVNQ FYTAPTAIRA 350
LMGQGKEFVE KCDLSDLKVL GTVGEPINPE AWNWYNDVVG KGKCPIVDTW 400
WQTETGGHLM TPLPGAHTMK PGSAMKPFFG IKPMVLEPAS GEVLEGNDVE 450
GVLVIADSWP GQMRTIWGDH ERFEKTYFSD YKGYYFTGDG CKRDADGDYW 500
ITGRVDDVIN VSGHRMGTAE VESALVAHAK VAEAAVVGYP HDIKGQGIYC 550
YVTLMNGEEP SDELYQELRK WVRAEIGPIA SPDLIQWAPG LPKTRSGKIM 600
RRILRKIAED DFATLGDTST LADPTVVDDL IKNRMNKQDA 640
Length:640
Mass (Da):70,426
Last modified:July 25, 2006 - v1
Checksum:i892116E2437F2578
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000362 Genomic DNA. Translation: ABG30773.1.
RefSeqiYP_681459.1. NC_008209.1.

Genome annotation databases

EnsemblBacteriaiABG30773; ABG30773; RD1_1117.
GeneIDi4197563.
KEGGirde:RD1_1117.
PATRICi23360369. VBIRosDen86677_1079.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000362 Genomic DNA. Translation: ABG30773.1 .
RefSeqi YP_681459.1. NC_008209.1.

3D structure databases

ProteinModelPortali Q16B70.
SMRi Q16B70. Positions 11-634.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 375451.RD1_1117.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABG30773 ; ABG30773 ; RD1_1117 .
GeneIDi 4197563.
KEGGi rde:RD1_1117.
PATRICi 23360369. VBIRosDen86677_1079.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci RDEN375451:GJIZ-1047-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: ATCC 33942 / OCh 114.

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: June 11, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

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