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H2IS18

- H2IS18_RAHAC

UniProt

H2IS18 - H2IS18_RAHAC

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Protein

Acetyl-coenzyme A synthetase

Gene

acs

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.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.UniRule annotation

Catalytic activityi

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

Cofactori

Note: Magnesium.UniRule annotationSAAS annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei312 – 3121Coenzyme AUniRule annotation
Binding sitei336 – 3361Coenzyme AUniRule annotation
Binding sitei501 – 5011ATPUniRule annotation
Binding sitei516 – 5161ATPUniRule annotation
Binding sitei524 – 5241Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei527 – 5271ATPUniRule annotation
Metal bindingi538 – 5381Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi540 – 5401Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi543 – 5431Magnesium; via carbonyl oxygenUniRule annotation
Binding sitei585 – 5851Coenzyme AUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi388 – 3903ATPUniRule annotation
Nucleotide bindingi412 – 4176ATPUniRule 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 annotation, Metal-bindingUniRule annotationSAAS 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:acsUniRule annotation
Synonyms:acsAImported
Ordered Locus Names:Rahaq2_0411Imported
ORF Names:GRAQ_03773Imported
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-acetyllysineUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

AcetylationUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliH2IS18.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni192 – 1954Coenzyme A bindingUniRule annotation

Sequence similaritiesi

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

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

« Hide

        10         20         30         40         50
MSHVYKHPIP ASVAERTLIT PEKYQQYYQQ SVEDPDAFWG EQAKVLDWIK
60 70 80 90 100
PFTKVKNTSF APGNVDIRWF EDGTLNLAAN CLDRHLTDKG DQTALVWEGD
110 120 130 140 150
DPKAENKYVT YKQLHHDVCQ FANVLKGLGV KKGDVVAIYM PMVPEAAVAM
160 170 180 190 200
LACARIGAVH SVIFAGFSPE AVAGRIVDSN AKLVITADEG LRAGRTIPLK
210 220 230 240 250
QNVDDALKNP AVTSITHSII FKRTGKQGEW KEGRDIWWHD AIEGVSADCP
260 270 280 290 300
PEEMKAEDPL FILYTSGSTG KPKGVLHTTG GYLVYAALTF KYTFDYHDGD
310 320 330 340 350
IYWCTADVGW VTGHSYLLYG PLACGAISLM FEGVPNYPTP ARMAQVIDKH
360 370 380 390 400
KVNILYTAPT AIRALMAEGD KAIEGTSRAS LRIMGSVGEP INPEAWEWYY
410 420 430 440 450
KTIGNSQCPI VDTWWQTETG GFMITPLPGA TELKAGSATR PFFGVQPALV
460 470 480 490 500
DNEGVPQEGA CEGNLVITDS WPGQARTLFG DHERFEQTYF STFKNMYFSG
510 520 530 540 550
DGARRDEDGY YWITGRVDDV LNISGHRLGT AEIESALVSH PKIAEAAVVG
560 570 580 590 600
IPHNIKGQAI YAYITLNHGE EPSPELYTEV RNWVRKEIGS IATPDILHWT
610 620 630 640 650
DSLPKTRSGK IMRRILRKIA AGDTSNLGDT STLADPGVVD KLLEEKQSMK

VPS
Length:653
Mass (Da):72,038
Last modified:March 21, 2012 - v1
Checksum:iE00B70418C59D169
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003244 Genomic DNA. Translation: AEX50349.1.
JMPO01000135 Genomic DNA. Translation: KFD01425.1.
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:
EMBLi
GenBanki
DDBJi
Links Updated
CP003244 Genomic DNA. Translation: AEX50349.1 .
JMPO01000135 Genomic DNA. Translation: KFD01425.1 .
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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: CIP 78.65Imported.
  2. "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 78.65Imported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: CIP 78.65Imported.
  4. "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of the evolutionary history of the Enterobacteriaceae."
    Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.
    Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ATCC 33071Imported.

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: November 26, 2014
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3