O45218 (ADAS_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alkyldihydroxyacetonephosphate synthase
Short name=Alkyl-DHAP synthase
EC=2.5.1.26

Alternative name(s):
Alkylglycerone-phosphate synthase

Gene names

Name:	ads-1
ORF Names:	Y50D7A.7

Organism

Caenorhabditis elegans

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	597 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	1-acyl-glycerone 3-phosphate + a long-chain alcohol = an alkyl-glycerone 3-phosphate + a long-chain acid anion.
Cofactor	FAD By similarity.
Pathway	Glycerolipid metabolism; ether lipid biosynthesis.
Subcellular location	Peroxisome.
Sequence similarities	Belongs to the FAD-binding oxidoreductase/transferase type 4 family. Contains 1 FAD-binding PCMH-type domain.

Ontologies

Keywords
Biological process	Lipid synthesis
Cellular component	Peroxisome
Ligand	FAD Flavoprotein
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	embryo development ending in birth or egg hatching Inferred from mutant phenotype. Source: WormBase growth Inferred from mutant phenotype. Source: WormBase lipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW nematode larval development Inferred from mutant phenotype. Source: WormBase
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	UDP-N-acetylmuramate dehydrogenase activity Inferred from electronic annotation. Source: InterPro alkylglycerone-phosphate synthase activity Inferred from electronic annotation. Source: EC flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 597	597	Alkyldihydroxyacetonephosphate synthase		PRO_0000128177
Regions
	Domain	131 – 313	183	FAD-binding PCMH-type
	Motif	595 – 597	3	Microbody targeting signal Potential
Sites
	Active site	507	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	O45218 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 6224D6A11E0811AB	FASTA	597	66,559
	10 20 30 40 50 60 MSASYQTIEH DVPQSYRDKI LKWNGWGYSD SQFAINKDGH VTFTGDKYEI SGKVMPHFRP 70 80 90 100 110 120 WFENYLGIDL GFVSPAQKLS DVIIDAPVEN EDIIEFLQEN KISFSNEARI RLMRGHGHTV 130 140 150 160 170 180 HDMINLREGK IPRLPDIVVW PKSEHEIVKI IEGAMSHNCA IIPIGGGTSV TNALDTPETE 190 200 210 220 230 240 KRAVISMDMA LLDKILWIDR ENLTCRAQAG IVGQSLERQL NKKGFTCGHE PDSIEFSTLG 250 260 270 280 290 300 GWVSTRASGM KKNKYGNIED LVVHLNFVCP KGIIQKQCQV PRMSSGPDIH QIILGSEGTL 310 320 330 340 350 360 GVVSEVTIKI FPIPEVKRFG SFVFPNFESG VNFFREVAIQ RCQPASLRLM DNDQFVMGQA 370 380 390 400 410 420 LKVASDSWWA DLKSSVSKMY ITSWKGFKVD EICAATCVYE GNREEVDQHE ERLNKLAEQF 430 440 450 460 470 480 HGVVGGAENG QYGYRLTFAI AYLRDLGMNH GVLGESFETS VPWDKVLSLC RNVKELMKRE 490 500 510 520 530 540 AKAQGVTHPV LANCRVTQVY DAGACVYFYF GFNARGLKNG LEVYDRIETA ARDEIIACGG 550 560 570 580 590 SISHHHGVGK IRKQWMLTTN GAVGIALLKA IKSELDPANI FASANLIDII GSPHCKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of a cDNA clone encoding a Caenorhabditis elegans homolog of mammalian alkyl-dihydroxyacetonephosphate synthase: evolutionary switching of peroxisomal targeting signals." de Vet E.C.J.M., Prinsen H.C.M.T., van den Bosch H. Biochem. Biophys. Res. Commun. 242:277-281(1998) [PubMed: 9446784] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ002686 mRNA. Translation: CAA05690.1. FO081772 Genomic DNA. Translation: CCD73794.1.
PIR	JC5829.
RefSeq	NP_497185.1. NM_064784.6.
UniGene	Cel.7909.
3D structure databases
ProteinModelPortal	O45218.
SMR	O45218. Positions 12-586.
ModBase	Search...
Protein-protein interaction databases
STRING	O45218.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	Y50D7A.7.1; Y50D7A.7.1; Y50D7A.7. Y50D7A.7.2; Y50D7A.7.2; Y50D7A.7.
GeneID	175192.
KEGG	cel:Y50D7A.7.
NMPDR	fig|6239.3.peg.8439.
UCSC	Y50D7A.7.1. c. elegans.
Organism-specific databases
CTD	175192.
WormBase	Y50D7A.7; CE26144; WBGene00000081; ads-1.
Phylogenomic databases
eggNOG	meNOG05588.
GeneTree	EMGT00050000009969.
HOGENOM	HBG383004.
InParanoid	O45218.
OMA	YNDSKFF.
PhylomeDB	O45218.
Gene expression databases
ArrayExpress	O45218.
Family and domain databases
InterPro	IPR016166. FAD-bd_2. IPR016167. FAD-bd_2_sub1. IPR016164. FAD-linked_Oxase-like_C. IPR016168. FAD-linked_Oxase_FAD-bd_sub2. IPR004113. FAD-linked_oxidase_C. IPR006094. Oxid_FAD_bind_N. IPR016171. Vanillyl_alc_oxidase_C-sub2. [Graphical view]
Gene3D	G3DSA:3.30.43.10. FAD-binding_2_sub1. 1 hit. G3DSA:3.30.465.20. FAD-linked_oxidase_FAD-bd_sub2. 1 hit. G3DSA:1.10.45.10. Vanillyl_alc_oxidase_C-sub2. 1 hit.
KO	K00803.
Pfam	PF02913. FAD-oxidase_C. 1 hit. PF01565. FAD_binding_4. 1 hit. [Graphical view]
SUPFAM	SSF55103. FAD-binding_2. 1 hit. SSF56176. FAD-binding_2. 1 hit.
PROSITE	PS51387. FAD_PCMH. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	887138.

Entry information

Entry name

ADAS_CAEEL

Accession

Primary (citable) accession number: O45218

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	June 1, 1998
Last modified:	December 14, 2011
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project