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E6WHR8

- E6WHR8_PANSA

UniProt

E6WHR8 - E6WHR8_PANSA

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Protein

Acetyl-coenzyme A synthetase

Gene

acs

Organism
Pantoea sp. (strain At-9b)
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 sitei311 – 3111Coenzyme AUniRule annotation
Binding sitei335 – 3351Coenzyme AUniRule annotation
Binding sitei500 – 5001ATPUniRule annotation
Binding sitei515 – 5151ATPUniRule annotation
Binding sitei523 – 5231Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei526 – 5261ATPUniRule annotation
Metal bindingi537 – 5371Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi539 – 5391Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi542 – 5421Magnesium; via carbonyl oxygenUniRule annotation
Binding sitei584 – 5841Coenzyme AUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi387 – 3893ATPUniRule annotation
Nucleotide bindingi411 – 4166ATPUniRule 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

Enzyme and pathway databases

BioCyciPSP592316:GI0L-347-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 ligaseUniRule annotation
Acyl-activating enzymeUniRule annotation
Gene namesi
Name:acsUniRule annotation
Ordered Locus Names:Pat9b_0328Imported
OrganismiPantoea sp. (strain At-9b)Imported
Taxonomic identifieri592316 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePantoea
ProteomesiUP000001624: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei609 – 6091N6-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

ProteinModelPortaliE6WHR8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni191 – 1944Coenzyme A bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000229981.
KOiK01895.
OMAiAWIWYRD.

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.

E6WHR8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSQIHKHPVP AAIAENALIN AEQYAAMYQQ SVDDPETFWG EQGKILDWIT
60 70 80 90 100
PYSKVKNTSF APGNVAIRWY EDGTLNLAAN CLDRHLASRG DHPAIIWEGD
110 120 130 140 150
DANESKTLTF RQLHADVCRF ANVLGSLGVK KGDVVAIYMP MVPEAAIAML
160 170 180 190 200
ACARIGAVHS VIFGGFSPEA VAGRIIDSNA KLVITADEGI RAGRGIPLKK
210 220 230 240 250
NVDDALNNPN VTSVKNVVVF KRTGKDTGWR EGRDLWWHDL MADAADQHQP
260 270 280 290 300
VAMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAATTFK YVFDYHPEDV
310 320 330 340 350
YWCTADVGWV TGHSYLIYGP LACGATTLMF EGVPNWPKPS RMAEVVDKHK
360 370 380 390 400
VTLLYTAPTA IRALMAEGDK AIEGTDRSSL RIMGSVGEPI NPEAWEWYYN
410 420 430 440 450
KIGDGRCPIV DTWWQTETGG FMITPLPGAI ELKAGSATKP FFGVQPALVD
460 470 480 490 500
NEGNTLEGAT EGNLVIVDSW PGQARTLFGD HDRFEQTYFS TFKNRYFSGD
510 520 530 540 550
GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVSHP KIAEAAVVGI
560 570 580 590 600
PHSIKGQAIY AYITLNHGEE PSPELYTEVR NWVRKEIGPI ATPDVLHWTD
610 620 630 640 650
SLPKTRSGKI MRRILRKIAT GDTSNLGDTS TLADPGVVEK LLEEKQSIKM

P
Length:651
Mass (Da):71,523
Last modified:March 8, 2011 - v1
Checksum:iF10BEEDD2003560E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002433 Genomic DNA. Translation: ADU67654.1.
RefSeqiWP_013507523.1. NC_014837.1.
YP_004114210.1. NC_014837.1.

Genome annotation databases

EnsemblBacteriaiADU67654; ADU67654; Pat9b_0328.
GeneIDi10067726.
KEGGipao:Pat9b_0328.
PATRICi45314927. VBIPanSp129740_0326.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002433 Genomic DNA. Translation: ADU67654.1 .
RefSeqi WP_013507523.1. NC_014837.1.
YP_004114210.1. NC_014837.1.

3D structure databases

ProteinModelPortali E6WHR8.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADU67654 ; ADU67654 ; Pat9b_0328 .
GeneIDi 10067726.
KEGGi pao:Pat9b_0328.
PATRICi 45314927. VBIPanSp129740_0326.

Phylogenomic databases

HOGENOMi HOG000229981.
KOi K01895.
OMAi AWIWYRD.

Enzyme and pathway databases

BioCyci PSP592316:GI0L-347-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. "Complete sequence chromosome of Pantoea sp. At-9b."
    US DOE Joint Genome Institute
    Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pinto A., Currie C., Woyke T.
    Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: At-9bImported.

Entry informationi

Entry nameiE6WHR8_PANSA
AccessioniPrimary (citable) accession number: E6WHR8
Entry historyi
Integrated into UniProtKB/TrEMBL: March 8, 2011
Last sequence update: March 8, 2011
Last modified: November 26, 2014
This is version 28 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