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Q3YY21 (AAS_SHISS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. 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:SSON_2996
OrganismShigella sonnei (strain Ss046) [Complete proteome] [HAMAP]
Taxonomic identifier300269 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

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_1000065644

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
Q3YY21 [UniParc].

Last modified September 27, 2005. Version 1.
Checksum: 139EBA7043BE21FB

FASTA71980,740
        10         20         30         40         50         60 
MLFSFFRNLC RVLYRVRVTG DTQALKGERV LITPNHVSFI DGILLGLFLP VRPVFAVYTS 

        70         80         90        100        110        120 
ISQQWYMRWL KSFIDFVPLD PTQPMAIKHL VRLVEQGRPV VIFPEGRITT TGSLMKIYDG 

       130        140        150        160        170        180 
AGFVAAKSGA TVIPVRIEGA ELTHFSRLKG LVKRRLFPQI TLHILPPTQV EMPDAPRARD 

       190        200        210        220        230        240 
RRKIAGEMLH QIMMEARMAV RPRETLYESL LSAMYRFGAG KKCVEDVNFT PDSYRKLLTK 

       250        260        270        280        290        300 
TLFVGRILEK YSVEGERIGL MLPNAGISAA VIFGAIARRR IPAMMNYTAG VKGLTSAITA 

       310        320        330        340        350        360 
AEIKTIFTSR QFLDKGKLWH LPEQLTQVRW VYLEDLKADV TTADKVWIFA HLLMPRLAQV 

       370        380        390        400        410        420 
KQQPEEEALI LFTSGSEGHP KGVVHSHKSI LANVEQIKTI ADFTTNDRFM SALPLFHSFG 

       430        440        450        460        470        480 
LTVGLFTPLL TGAEVFLYPS PLHYRIVPEL VYDRSCTVLF GTSTFLGHYA RFANPYDFYR 

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

       550        560        570        580        590        600 
DARLLSVPGI EEGGRLQLKG PNIMNGYLRV EKPGVLEVPT AENVRGEMER GWYDTGDIVR 

       610        620        630        640        650        660 
FDEQGFVQIQ GRAKRFAKIA GEMVSLEMVE QLALGVSPDK VHATAIKSDA SKGEALVLFT 

       670        680        690        700        710 
TDNELTRDKL QQYAREHGVP ELAVPRDIRY LKQMPLLGSG KPDFVTLKSW VDEAEQHDE 

« Hide

References

[1]"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery."
Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J. expand/collapse author list , Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q.
Nucleic Acids Res. 33:6445-6458(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ss046.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000038 Genomic DNA. Translation: AAZ89591.1.
RefSeqYP_311826.1. NC_007384.1.

3D structure databases

ProteinModelPortalQ3YY21.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING300269.SSON_2996.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ89591; AAZ89591; SSON_2996.
GeneID3668171.
KEGGssn:SSON_2996.
PATRIC18740519. VBIShiSon107113_3565.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSSON300269:GJJF-2991-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_SHISS
AccessionPrimary (citable) accession number: Q3YY21
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: September 27, 2005
Last modified: February 19, 2014
This is version 58 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