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F4DQJ9

- F4DQJ9_PSEMN

UniProt

F4DQJ9 - F4DQJ9_PSEMN

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Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Pseudomonas mendocina (strain NK-01)
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.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: InterPro
Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotation

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciPMEN1001585:GIWS-3446-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:acsAUniRule annotation
Ordered Locus Names:MDS_3395Imported
OrganismiPseudomonas mendocina (strain NK-01)Imported
Taxonomic identifieri1001585 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000008306: 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

ProteinModelPortaliF4DQJ9.
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

KOiK01895.
OMAiDISWING.

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.

F4DQJ9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSAASLYPVR PEVAARTLTD EATYKAMYQQ SVVNPEGFWR EQGKRIDWIK
60 70 80 90 100
PYTKVKQTTF DDHHVDIKWY ADGTLNVSYN CLDRHLEERG DQVAIIWEGD
110 120 130 140 150
DPSEHREITY RQLHEEVSKF ANALRGQDVH RGDVVTIYMP MIPEAVVAML
160 170 180 190 200
ACARIGAIHS VVFGGFSPEA LAGRIIDCES KVVITADEGL RGGRKVPLKA
210 220 230 240 250
NVDDALTNPE TASVQKIIVV KRTGSDIKWN QHRDIWYEDL MKVAGSVCAP
260 270 280 290 300
KEMGAEEALF ILYTSGSTGK PKGVLHTTGG YLTYASLTHE RVFDYRPGEV
310 320 330 340 350
FWCTADIGWV TGHTYLVYGP LSNGATTLMF EGVPNYPDVR RVAQIVDKHK
360 370 380 390 400
VNILYTAPTA IRAMMAEGKA AVEGADGSSL RLLGSVGEPI NPEAWQWYYE
410 420 430 440 450
NVGQSRCPIV DTWWQTETGA CLMTPLPGAH GLKPGSAARP FFGVQPALVD
460 470 480 490 500
NLGNIIEGPA EGNLVIIDSW PGQARTLYGD HDRFVDTYFK TFRGMYFTGD
510 520 530 540 550
GARRDEDGYW WITGRVDDVL NVSGHRMGTA EVESAMVAHP KVAEAAVVGV
560 570 580 590 600
PHDIKGQGIY VYVTLNAGEE SSEQLRQELK NWVRKEIGPI ATPDVIQWAP
610 620 630 640 650
GLPKTRSGKI MRRILRKIAT AEYDSLGDIS TLADPGVVQH LIDTHRQMQA

ACA
Length:653
Mass (Da):72,265
Last modified:June 28, 2011 - v1
Checksum:iFAD6AE26483A4D3D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002620 Genomic DNA. Translation: AEB59426.1.
RefSeqiYP_004381178.1. NC_015410.1.

Genome annotation databases

EnsemblBacteriaiAEB59426; AEB59426; MDS_3395.
GeneIDi10458177.
KEGGipmk:MDS_3395.
PATRICi54487546. VBIPseMen187712_3448.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002620 Genomic DNA. Translation: AEB59426.1 .
RefSeqi YP_004381178.1. NC_015410.1.

3D structure databases

ProteinModelPortali F4DQJ9.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AEB59426 ; AEB59426 ; MDS_3395 .
GeneIDi 10458177.
KEGGi pmk:MDS_3395.
PATRICi 54487546. VBIPseMen187712_3448.

Phylogenomic databases

KOi K01895.
OMAi DISWING.

Enzyme and pathway databases

BioCyci PMEN1001585:GIWS-3446-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 genome of Pseudomonas mendocina NK-01, which synthesizes medium-chain-length polyhydroxyalkanoates and alginate oligosaccharides."
    Guo W., Wang Y., Song C., Yang C., Li Q., Li B., Su W., Sun X., Song D., Yang X., Wang S.
    J. Bacteriol. 193:3413-3414(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NK-01Imported.

Entry informationi

Entry nameiF4DQJ9_PSEMN
AccessioniPrimary (citable) accession number: F4DQJ9
Entry historyi
Integrated into UniProtKB/TrEMBL: June 28, 2011
Last sequence update: June 28, 2011
Last modified: November 26, 2014
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3