Reviewed, UniProtKB/Swiss-Prot P97275 (ADAS_CAVPO)

Names and origin

Protein names

Recommended name:
    Alkyldihydroxyacetonephosphate synthase, peroxisomal
      Short name=Alkyl-DHAP synthase
    EC=2.5.1.26
Alternative name(s):
    Alkylglycerone-phosphate synthase

Gene names

Name:

AGPS

Organism

Cavia porcellus (Guinea pig)

Taxonomic identifier

10141 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Hystricognathi › Caviidae › Cavia

Protein attributes

Sequence length	658 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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.
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
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Transferase
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	lipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro alkylglycerone-phosphate synthase activity Inferred from electronic annotation. Source: EC oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 58	58	Peroxisome Ref.1
	Chain	59 – 658	600	Alkyldihydroxyacetonephosphate synthase, peroxisomal		PRO_0000020430
Regions
	Domain	202 – 384	183	FAD-binding PCMH-type
	Compositional bias	2 – 14	13	Poly-Ala
Sites
	Active site	578	1	By similarity
Amino acid modifications
	Modified residue	65	1	Phosphoserine By similarity
	Modified residue	102	1	N6-acetyllysine By similarity
	Modified residue	169	1	N6-acetyllysine By similarity
	Modified residue	347	1	N6-acetyllysine By similarity
Experimental info
	Mutagenesis	300	1	H → A: Loss of activity. Ref.2
	Mutagenesis	367	1	S → A: Strongly reduced activity. Ref.2
	Mutagenesis	419	1	R → H: Loss of activity. Ref.2
	Mutagenesis	419	1	R → K: Strongly reduced activity. Ref.2
	Mutagenesis	615	1	H → A: Loss of activity. Ref.2
	Mutagenesis	616	1	H → A: Loss of activity. Ref.2
	Mutagenesis	617	1	H → A: Loss of activity. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P97275-1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: B6272EB407EBB5F1	FASTA	658	72,846
	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

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: 8995366] [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: 10692424] [Abstract] Cited for: CHARACTERIZATION, MUTAGENESIS OF HIS-300; SER-367; ARG-419; HIS-615; HIS-616 AND HIS-617.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Y08826 mRNA. Translation: CAA70060.1.
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	ENSCPOT00000000684; ENSCPOP00000000601; ENSCPOG00000000679; Cavia porcellus. [Genome view]
Phylogenomic databases
HOVERGEN	P97275.
OMA	FFFNKKG.
Enzyme and pathway databases
BRENDA	2.5.1.26. 44.
Family and domain databases
InterPro	IPR016166. FAD-bd_2. IPR016167. FAD-bd_2_sub1. IPR016168. FAD-linked_Oxase_FAD-bd_sub2. IPR004113. FAD-linked_oxidase_C. IPR006094. Oxid_FAD_bind_N. [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.
Pfam	PF02913. FAD-oxidase_C. 1 hit. PF01565. FAD_binding_4. 1 hit. [Graphical view]
PROSITE	PS51387. FAD_PCMH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ADAS_CAVPO

Accession

Primary (citable) accession number: P97275

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 1, 1997
Last modified:	November 3, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)