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B1JQC1 (AAS_YERPY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional protein Aas

Including the following 2 domains:

  1. 2-acylglycerophosphoethanolamine acyltransferase
    EC=2.3.1.40
    Alternative name(s):
    2-acyl-GPE acyltransferase
    Acyl-[acyl-carrier-protein]--phospholipid O-acyltransferase
  2. Acyl-[acyl-carrier-protein] synthetase
    EC=6.2.1.20
    Alternative name(s):
    Acyl-ACP synthetase
    Long-chain-fatty-acid--[acyl-carrier-protein] ligase
Gene names
Name:aas
Ordered Locus Names:YPK_1027
OrganismYersinia pseudotuberculosis serotype O:3 (strain YPIII) [Complete proteome] [HAMAP]
Taxonomic identifier502800 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length718 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1 By similarity. HAMAP-Rule MF_01162

Catalytic activity

Acyl-[acyl-carrier-protein] + O-(2-acyl-sn-glycero-3-phospho)ethanolamine = [acyl-carrier-protein] + O-(1-beta-acyl-2-acyl-sn-glycero-3-phospho)ethanolamine. HAMAP-Rule MF_01162

ATP + an acid + [acyl-carrier-protein] = AMP + diphosphate + acyl-[acyl-carrier-protein]. HAMAP-Rule MF_01162

Subcellular location

Cell inner membrane; Multi-pass membrane protein By similarity HAMAP-Rule MF_01162.

Sequence similarities

In the N-terminal section; belongs to the 2-acyl-GPE acetyltransferase family.

In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 718718Bifunctional protein Aas HAMAP-Rule MF_01162
PRO_1000137906

Regions

Transmembrane258 – 27720Helical; Potential
Transmembrane409 – 43325Helical; Potential
Region15 – 138124Acyltransferase HAMAP-Rule MF_01162
Region233 – 646414AMP-binding HAMAP-Rule MF_01162

Sites

Active site361 By similarity

Sequences

Sequence LengthMass (Da)Tools
B1JQC1 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: A3C7873868B30645

FASTA71879,416
        10         20         30         40         50         60 
MAYRLLRALF RGLFRVTIDG VTDQFKHEKL IITPNHVSFL DGALLALFLP IKPVFAVYTS 

        70         80         90        100        110        120 
ITDTWYMRWL KPYVDFVALD PTNPMAIKHL VRMVEQGRPV VIFPEGRITV TGSLMKIYDG 

       130        140        150        160        170        180 
AAFVAAKSGA AVVPIRLDGP EFTHFGRLQG VLKTRWFPKI SIHVLPATTI PMPQAPRSRE 

       190        200        210        220        230        240 
RRVLAGEHLH TIMMAARMAT VPRETLFEAL LSAQTRYGRF KPCIEDVSFK EDSYQTLLKK 

       250        260        270        280        290        300 
TLGVSRILQR FTVPGEHVGM LLPNATITAA AIFGASLRGR IPALLNYTSG AKGLQSAIIA 

       310        320        330        340        350        360 
ASLKTIVTSR QFLEKGKLTH LPEQVNEVNW VYLEDLKDTV TLTDKLWILF HLCFPRRAML 

       370        380        390        400        410        420 
PQQADDSALI LFTSGSEGNP KGVVHSHASL LANVEQIRTI ADFTPRDRFM SSLPLFHAFG 

       430        440        450        460        470        480 
LTVGLFTPLM TGSRVFLYPS PLHYRVVPEL VYDRNCTVLF GTSTFLGNYA RFAHPYDFAR 

       490        500        510        520        530        540 
VRYVVAGAEK LAESTKQIWQ DKFGIRILEG YGVTECAPVV AINVPMAAKV NTVGRILPGM 

       550        560        570        580        590        600 
EARLINVPGI AQGGRLQLRG PNIMRGYLRV ENPGVLEQPS AENAQGELDA NWYDTGDIVT 

       610        620        630        640        650        660 
LDEQGFCAIR GRVKRFAKLA GEMVSLESVE QLAISLSPEG QHAAAAKTDS AKGEALVLFT 

       670        680        690        700        710 
TDSEITRERL IKAARENGVP ELAVPRDIRV VKALPLLGSG KPDFVTLGKM AQDPEMSV 

« Hide

References

[1]"Complete sequence of Yersinia pseudotuberculosis YPIII."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YPIII.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000950 Genomic DNA. Translation: ACA67328.1.
RefSeqYP_001719781.1. NC_010465.1.

3D structure databases

ProteinModelPortalB1JQC1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING502800.YPK_1027.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA67328; ACA67328; YPK_1027.
GeneID6089685.
KEGGypy:YPK_1027.
PATRIC18659194. VBIYerPse127545_1101.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0318.
HOGENOMHOG000004907.
KOK05939.
OMAANWVYLE.
OrthoDBEOG6KHFVG.
ProtClustDBPRK08043.

Enzyme and pathway databases

BioCycYPSE502800:GH0W-1037-MONOMER.

Family and domain databases

HAMAPMF_01162. Aas.
InterProIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR023775. Bifunctional_Aas.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamPF01553. Acyltransferase. 1 hit.
PF00501. AMP-binding. 1 hit.
[Graphical view]
SMARTSM00563. PlsC. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAAS_YERPY
AccessionPrimary (citable) accession number: B1JQC1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: February 19, 2014
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families