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P97275 (ADAS_CAVPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alkyldihydroxyacetonephosphate synthase, peroxisomal
Short name=Alkyl-DHAP synthase
EC=2.5.1.26
Alternative name(s):
Alkylglycerone-phosphate synthase
Gene names
Name:AGPS
OrganismCavia porcellus (Guinea pig) [Reference proteome]
Taxonomic identifier10141 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Hystricognathi › Caviidae › Cavia

Protein attributes

Sequence length658 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the exchange of an acyl for a long-chain alkyl group and the formation of the ether bond in the biosynthesis of ether phospholipids. Ref.3

Catalytic activity

1-acyl-glycerone 3-phosphate + a long-chain alcohol = an alkyl-glycerone 3-phosphate + a long-chain acid anion. Ref.3

Cofactor

FAD. Ref.3

Pathway

Glycerolipid metabolism; ether lipid biosynthesis.

Subunit structure

Homodimer. Ref.3

Subcellular location

Peroxisome.

Sequence similarities

Belongs to the FAD-binding oxidoreductase/transferase type 4 family.

Contains 1 FAD-binding PCMH-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5858Peroxisome Ref.1
Chain59 – 658600Alkyldihydroxyacetonephosphate synthase, peroxisomal
PRO_0000020430

Regions

Domain202 – 384183FAD-binding PCMH-type
Nucleotide binding234 – 2407FAD
Nucleotide binding303 – 3097FAD
Nucleotide binding316 – 3194FAD
Nucleotide binding368 – 3747FAD
Region615 – 6173Important for enzyme activity
Compositional bias2 – 1413Poly-Ala

Sites

Active site5781Proton donor/acceptor Ref.3
Binding site5151Substrate
Site4191Important for enzyme activity

Amino acid modifications

Modified residue651Phosphoserine By similarity
Modified residue1021N6-acetyllysine By similarity
Modified residue3471N6-acetyllysine By similarity

Experimental info

Mutagenesis3001H → A: Loss of activity. Ref.2
Mutagenesis3091T → I: Impaired FAD binding and protein stability. Loss of activity. Ref.3
Mutagenesis3671S → A: Strongly reduced activity. Ref.2
Mutagenesis4191R → H: Loss of activity. Ref.2 Ref.3
Mutagenesis4191R → K: Strongly reduced activity. Ref.2 Ref.3
Mutagenesis4691L → P: Impaired FAD binding and protein stability. Loss of activity. Ref.3
Mutagenesis5151R → L: Impaired FAD binding and protein stability. Loss of activity. Ref.3
Mutagenesis5781Y → F: Loss of activity. Ref.3
Mutagenesis6151H → A: Loss of activity. Ref.2
Mutagenesis6161H → A: Loss of activity. Ref.2
Mutagenesis6171H → A: Loss of activity. Ref.2

Secondary structure

1 ........................................................................................... 658
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P97275 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: B6272EB407EBB5F1

FASTA65872,846
        10         20         30         40         50         60 
MAEAAAAAAA AAAAGETSAS SGSAAERDPD QDRAGRRLRV LSGHLLGRPQ EALSTNECKA 

        70         80         90        100        110        120 
RRAASAATAA PTATPAAPES GIIPKKRQEL MKWNGWGYND SKFFLNKKGQ LELTGKRYPL 

       130        140        150        160        170        180 
SGVALPTFKD WIQNTFGINL DHKTTSKASL NPSDTPPSIV NEDFLHELKK TNISYSQEAD 

       190        200        210        220        230        240 
DRVFRAHGHC LHEIFLLREG MFERIPDIVL WPTCHDDVVK IVNLACKYNL CIIPIGGGTS 

       250        260        270        280        290        300 
VSYGLMCPAD ETRTIISLDT SQMNRILWVD ENNLTAHVEA GITGQELERQ LKESGYCTGH 

       310        320        330        340        350        360 
EPDSLEFSTV GGWISTRASG MKKNIYGNIE DLVVHMKVVT PRGVIEKSCQ GPRMSTGPDI 

       370        380        390        400        410        420 
HHFIMGSEGT LGVITEATIK IRPTPEYQKY GSVAFPNFEQ GVACLREIAK QRCAPASIRL 

       430        440        450        460        470        480 
MDNQQFQFGH ALKPQVSSIF TSFLDGLKKF YITKFKGFDP NQLSVATLLF EGDREKVLQH 

       490        500        510        520        530        540 
EKQVYDIAAK FGGLAAGEDN GQRGYLLTYV IAYMRDLGLE YYIIGESFET SAPWDRVVDL 

       550        560        570        580        590        600 
CRNVKERIRR ECKEKGVQFP PLSTCRVTQT YDAGACIYFY FAFNYRGISD PLAVFEQTEA 

       610        620        630        640        650 
AAREEILANG GSLSHHHGVG KLRKQWLKES ISDVGFGMLK SVKDYVDPTN IFGNRNLL

« Hide

References

[1]"Polymerase chain reaction-based cloning of alkyl-dihydroxyacetonephosphate synthase complementary DNA from guinea pig liver."
de Vet E.C.J.M., Zomer A.W.M., Lahaut G.J.H.T.J., van den Bosch H.
J. Biol. Chem. 272:798-803(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 59-83; 92-114; 422-445 AND 515-539.
Tissue: Liver.
[2]"Alkyl-dihydroxyacetonephosphate synthase. Presence and role of flavin adenine dinucleotide."
de Vet E.C.J.M., Hilkes Y.H.A., Fraaije M.W., van den Bosch H.
J. Biol. Chem. 275:6276-6283(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, MUTAGENESIS OF HIS-300; SER-367; ARG-419; HIS-615; HIS-616 AND HIS-617.
[3]"Precursor of ether phospholipids is synthesized by a flavoenzyme through covalent catalysis."
Nenci S., Piano V., Rosati S., Aliverti A., Pandini V., Fraaije M.W., Heck A.J., Edmondson D.E., Mattevi A.
Proc. Natl. Acad. Sci. U.S.A. 109:18791-18796(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF WILD-TYPE AND MUTANTS HIS-419 AND PHE-578 IN COMPLEX WITH FAD AND SUBSTRATE ANALOG, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ACTIVE SITE, COFACTOR, MUTAGENESIS OF THR-309; ARG-419; LEU-469; ARG-515 AND TYR-578.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y08826 mRNA. Translation: CAA70060.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4BBYX-ray1.90A/B/C/D1-658[»]
4BC7X-ray2.40A/B/C/D1-658[»]
4BC9X-ray2.41A/B/C/D1-658[»]
4BCAX-ray2.40A/B/C/D1-658[»]
ProteinModelPortalP97275.
ModBaseSearch...

Protein-protein interaction databases

STRING10141.ENSCPOP00000000601.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSCPOT00000000684; ENSCPOP00000000601; ENSCPOG00000000679.

Phylogenomic databases

eggNOGCOG0277.
GeneTreeENSGT00530000063515.
HOGENOMHOG000231620.
HOVERGENHBG004179.
InParanoidP97275.
OMAYLRDLGM.
OrthoDBEOG44XJGD.

Enzyme and pathway databases

SABIO-RKP97275.
UniPathwayUPA00781.

Family and domain databases

Gene3D3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProIPR025650. Alkyl-DHAP_Synthase.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR016164. FAD-linked_Oxase-like_C.
IPR004113. FAD-linked_oxidase_C.
IPR006094. Oxid_FAD_bind_N.
[Graphical view]
PANTHERPTHR11748:SF3. PTHR11748:SF3. 1 hit.
PfamPF02913. FAD-oxidase_C. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMSSF55103. FAD-binding_2. 1 hit.
SSF56176. FAD-binding_2. 1 hit.
PROSITEPS51387. FAD_PCMH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameADAS_CAVPO
AccessionPrimary (citable) accession number: P97275
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: April 3, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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