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Q02FT9

- Q02FT9_PSEAB

UniProt

Q02FT9 - Q02FT9_PSEAB

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Protein

Acetyl-coenzyme A synthetase

Gene

acsB

Organism
Pseudomonas aeruginosa (strain UCBPP-PA14)
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 sitei308 – 3081Coenzyme AUniRule annotation
Binding sitei332 – 3321Coenzyme AUniRule annotation
Binding sitei497 – 4971ATPUniRule annotation
Binding sitei512 – 5121ATPUniRule annotation
Binding sitei520 – 5201Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei523 – 5231ATPUniRule annotation
Metal bindingi534 – 5341Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi536 – 5361Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi539 – 5391Magnesium; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi384 – 3863ATPUniRule annotation
Nucleotide bindingi408 – 4136ATPUniRule 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

BioCyciPAER208963:GI5K-5113-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:acsBImported
Synonyms:acsAUniRule annotation
Ordered Locus Names:PA14_62630Imported
OrganismiPseudomonas aeruginosa (strain UCBPP-PA14)Imported
Taxonomic identifieri208963 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000000653: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei606 – 6061N6-acetyllysineUniRule annotation

Post-translational modificationi

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

Keywords - PTMi

AcetylationUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi208963.PA14_62630.

Structurei

3D structure databases

ProteinModelPortaliQ02FT9.
SMRiQ02FT9. Positions 7-642.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni190 – 1934Coenzyme A bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiRRIFEPT.
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.

Q02FT9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFEISVHPVP DAVRQRAYLN DDDYQRLYRQ SVENPDEFWS EQAKAFLDWF
60 70 80 90 100
KPWHSVHHGD LRKGQATWFK GGQLNVAYNC IDRHLERRGE QIAIVWEGDN
110 120 130 140 150
PSESAHITYR KLHHNVCRLA NVLKSRGVEK GDRVCIYMPM IPEAAYAMLA
160 170 180 190 200
CARIGAVHSV VFGGFSPDSL RDRILDADCR TVITADEGVR GGKYIPLKQN
210 220 230 240 250
VEKALKDCPD VSTVVVVERT QGDIPWVEGR DIWYHEALHA ASADCPAEAM
260 270 280 290 300
DAEDPLFILY TSGSTGKPKG VLHTTGGYLL GAAMTHKYVF DYHDGDVYWC
310 320 330 340 350
TADVGWVTGH SYIVYGPLAN GATTLMFEGV PNYPDASRFW QVIDKHQVNI
360 370 380 390 400
FYTAPTAIRA LMREGDAPVR QTSRSSLRLL GSVGEPINPE AWEWYYQVVG
410 420 430 440 450
EKRCPIVDTW WQTETGSILI TPLPGATALK PGSATRPFFG VQPVLLDEKG
460 470 480 490 500
KEIDGAGSGV LAIKASWPSQ IRSVYGDHQR MIDTYFKPYP GYYFSGDGAR
510 520 530 540 550
RDEDGYYWIT GRVDDVINVS GHRIGTAEVE SALVLHDAVA EAAVVGCPHD
560 570 580 590 600
VKGQAIYAFV TLMAGSQPSE ALQQELLALV GKEIGSFAKP DHLQWAPSLP
610 620 630 640
KTRSGKIMRR ILRKIACNEL DSLGDTSTLA DPGVVQGLID NRLNR
Length:645
Mass (Da):71,640
Last modified:November 14, 2006 - v1
Checksum:iD3F63891F880B1EA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000438 Genomic DNA. Translation: ABJ14116.1.
RefSeqiYP_793197.1. NC_008463.1.

Genome annotation databases

EnsemblBacteriaiABJ14116; ABJ14116; PA14_62630.
GeneIDi4383182.
KEGGipau:PA14_62630.
PATRICi19856442. VBIPseAer79785_5138.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000438 Genomic DNA. Translation: ABJ14116.1 .
RefSeqi YP_793197.1. NC_008463.1.

3D structure databases

ProteinModelPortali Q02FT9.
SMRi Q02FT9. Positions 7-642.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 208963.PA14_62630.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABJ14116 ; ABJ14116 ; PA14_62630 .
GeneIDi 4383182.
KEGGi pau:PA14_62630.
PATRICi 19856442. VBIPseAer79785_5138.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci PAER208963:GI5K-5113-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: UCBPP-PA14Imported.

Entry informationi

Entry nameiQ02FT9_PSEAB
AccessioniPrimary (citable) accession number: Q02FT9
Entry historyi
Integrated into UniProtKB/TrEMBL: November 14, 2006
Last sequence update: November 14, 2006
Last modified: November 26, 2014
This is version 52 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