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Q5PEN7 (AAS_SALPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 61. 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:SPA2875
OrganismSalmonella paratyphi A (strain ATCC 9150 / SARB42) [Complete proteome] [HAMAP]
Taxonomic identifier295319 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length719 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 – 719719Bifunctional protein Aas HAMAP-Rule MF_01162
PRO_0000193051

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
Q5PEN7 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 7CEB9BAEF7475651

FASTA71980,511
        10         20         30         40         50         60 
MLFGFFRNLF RVLYRVRVTG DVRALQGNRV LITPNHVSFI DGMLLALFLP VRPVFAVYTS 

        70         80         90        100        110        120 
ISQQWYMRWL TPLIDFVPLD PTKPMSIKHL MRLVEQGRPV VIFPEGRISV TGSLMKIYDG 

       130        140        150        160        170        180 
AGFVAAKSGA TVIPLRIDGA ELTPFSRLKG LVKRRLFPRI QLHILPPTQI PMPEAPRARD 

       190        200        210        220        230        240 
RRKIAGEMLH QIMMEARMAV RPRETLYESL LAAQYRYGAG KNCIEDINFT PDTYRKLLTK 

       250        260        270        280        290        300 
TLFVGRILEK YSVEGEKIGL MLPNAAISAA VIFGAVSRRR IPAMMNYTAG VKGLTSAIAA 

       310        320        330        340        350        360 
AEIKTIFTSR QFLDKGKLWH LPEQLTQVRW VYLEDLKADV TLADKLWIFA HLLAPRLAQV 

       370        380        390        400        410        420 
KQQPEDAAII LFTSGSEGHP KGVVHSHKSI LANVEQIKTI ADFTANDRFM SALPLFHSFG 

       430        440        450        460        470        480 
LTVGLFTPLL TGAEVFLYPS PLHYRIVPEL VYDRNCTVLF GTSTFLGNYA RFANPYDFYR 

       490        500        510        520        530        540 
LRYVVAGAEK LQESTKQLWQ DKFGLRILEG YGVTECAPVV SINVPMAAKP GTVGRILPGM 

       550        560        570        580        590        600 
DARLLAVPGI ENGGRLQLKG PNIMNGYLRV EKPGVLEVPS AENARGETER GWYDTGDIVR 

       610        620        630        640        650        660 
FDENGFVQIQ GRAKRFAKIA GEMVSLEMVE QLALGVSADK MHATAIKSDA SKGEALVLFT 

       670        680        690        700        710 
TDSELTREKL QHYAREHGIP ELAVPRDIRY LKQLPLLGSG KPDFVTLKSW VDAPEQHHE 

« Hide

References

[1]"Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid."
McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F. expand/collapse author list , Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L., Spieth J., Wilson R.K.
Nat. Genet. 36:1268-1274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9150 / SARB42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000026 Genomic DNA. Translation: AAV78720.1.
RefSeqYP_152032.1. NC_006511.1.

3D structure databases

ProteinModelPortalQ5PEN7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING295319.SPA2875.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV78720; AAV78720; SPA2875.
PATRIC32355319. VBISalEnt134188_3055.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0318.
HOGENOMHOG000004907.
OMAANWVYLE.
OrthoDBEOG6KHFVG.

Enzyme and pathway databases

BioCycSENT295319:GJBZ-2873-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_SALPA
AccessionPrimary (citable) accession number: Q5PEN7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: January 4, 2005
Last modified: May 14, 2014
This is version 61 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