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H2IS18

- H2IS18_RAHAC

UniProt

H2IS18 - H2IS18_RAHAC

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Protein

Acetyl-coenzyme A synthetase

Gene
acs, Rahaq2_0411
Organism
Rahnella aquatilis (strain ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 / CIP 78.65)
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. Acs undergoes a two-step reaction. In the first half reaction, Acs 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
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
Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis 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 sitei312 – 3121Coenzyme A By similarityUniRule annotation
Binding sitei336 – 3361Coenzyme A By similarityUniRule annotation
Binding sitei388 – 3881Substrate; via nitrogen amide By similarityUniRule annotation
Binding sitei501 – 5011Substrate By similarityUniRule annotation
Binding sitei516 – 5161Substrate By similarityUniRule annotation
Active sitei518 – 5181 By similarityUniRule annotation
Binding sitei524 – 5241Coenzyme A By similarityUniRule annotation
Binding sitei527 – 5271Substrate By similarityUniRule annotation
Metal bindingi538 – 5381Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi540 – 5401Magnesium; via carbonyl oxygen By similarityUniRule annotation
Metal bindingi543 – 5431Magnesium; via carbonyl oxygen By similarityUniRule annotation
Binding sitei585 – 5851Coenzyme 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: UniProtKB-HAMAP
  2. chemotaxis Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotationImported

Keywords - Ligandi

ATP-bindingUniRule annotation, MagnesiumUniRule annotationSAAS annotations, Metal-bindingUniRule annotationSAAS annotations, 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 ligase
Acyl-activating enzyme
Gene namesi
Name:acsUniRule annotation
Ordered Locus Names:Rahaq2_0411Imported
OrganismiRahnella aquatilis (strain ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 / CIP 78.65)Imported
Taxonomic identifieri745277 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeRahnella
ProteomesiUP000009010: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei610 – 6101N6-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

Structurei

3D structure databases

ProteinModelPortaliH2IS18.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni192 – 1954Coenzyme A By similarityUniRule annotation
Regioni412 – 4176Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Phylogenomic databases

KOiK01895.

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.

H2IS18-1 [UniParc]FASTAAdd to Basket

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MSHVYKHPIP ASVAERTLIT PEKYQQYYQQ SVEDPDAFWG EQAKVLDWIK    50
PFTKVKNTSF APGNVDIRWF EDGTLNLAAN CLDRHLTDKG DQTALVWEGD 100
DPKAENKYVT YKQLHHDVCQ FANVLKGLGV KKGDVVAIYM PMVPEAAVAM 150
LACARIGAVH SVIFAGFSPE AVAGRIVDSN AKLVITADEG LRAGRTIPLK 200
QNVDDALKNP AVTSITHSII FKRTGKQGEW KEGRDIWWHD AIEGVSADCP 250
PEEMKAEDPL FILYTSGSTG KPKGVLHTTG GYLVYAALTF KYTFDYHDGD 300
IYWCTADVGW VTGHSYLLYG PLACGAISLM FEGVPNYPTP ARMAQVIDKH 350
KVNILYTAPT AIRALMAEGD KAIEGTSRAS LRIMGSVGEP INPEAWEWYY 400
KTIGNSQCPI VDTWWQTETG GFMITPLPGA TELKAGSATR PFFGVQPALV 450
DNEGVPQEGA CEGNLVITDS WPGQARTLFG DHERFEQTYF STFKNMYFSG 500
DGARRDEDGY YWITGRVDDV LNISGHRLGT AEIESALVSH PKIAEAAVVG 550
IPHNIKGQAI YAYITLNHGE EPSPELYTEV RNWVRKEIGS IATPDILHWT 600
DSLPKTRSGK IMRRILRKIA AGDTSNLGDT STLADPGVVD KLLEEKQSMK 650
VPS 653
Length:653
Mass (Da):72,038
Last modified:March 21, 2012 - v1
Checksum:iE00B70418C59D169
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003244 Genomic DNA. Translation: AEX50349.1.
RefSeqiYP_005198489.1. NC_016818.1.

Genome annotation databases

EnsemblBacteriaiAEX50349; AEX50349; Rahaq2_0411.
GeneIDi11790113.
KEGGiraq:Rahaq2_0411.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003244 Genomic DNA. Translation: AEX50349.1 .
RefSeqi YP_005198489.1. NC_016818.1.

3D structure databases

ProteinModelPortali H2IS18.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AEX50349 ; AEX50349 ; Rahaq2_0411 .
GeneIDi 11790113.
KEGGi raq:Rahaq2_0411.

Phylogenomic databases

KOi K01895.

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. "Complete sequence of chromosome of Rahnella aquatilis CIP 78.65."
    Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sobecky P., Martinez R., Woyke T.
    Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 / CIP 78.65.

Entry informationi

Entry nameiH2IS18_RAHAC
AccessioniPrimary (citable) accession number: H2IS18
Entry historyi
Integrated into UniProtKB/TrEMBL: March 21, 2012
Last sequence update: March 21, 2012
Last modified: June 11, 2014
This is version 14 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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