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Alkyldihydroxyacetonephosphate synthase, peroxisomal (Alkyl-DHAP synthase) (EC 2.5.1.26) (Alkylglycerone-phosphate synthase)

 ADAS_CAVPO              Reviewed;         658 AA.
P97275;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
25-OCT-2017, entry version 103.
RecName: Full=Alkyldihydroxyacetonephosphate synthase, peroxisomal;
Short=Alkyl-DHAP synthase;
EC=2.5.1.26;
AltName: Full=Alkylglycerone-phosphate synthase;
Flags: Precursor;
Name=AGPS;
Cavia porcellus (Guinea pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
Hystricomorpha; Caviidae; Cavia.
NCBI_TaxID=10141;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 59-83; 92-114;
422-445 AND 515-539.
TISSUE=Liver;
PubMed=8995366; DOI=10.1074/jbc.272.2.798;
de Vet E.C.J.M., Zomer A.W.M., Lahaut G.J.H.T.J., van den Bosch H.;
"Polymerase chain reaction-based cloning of alkyl-
dihydroxyacetonephosphate synthase complementary DNA from guinea pig
liver.";
J. Biol. Chem. 272:798-803(1997).
[2]
CHARACTERIZATION, AND MUTAGENESIS OF HIS-300; SER-367; ARG-419;
HIS-615; HIS-616 AND HIS-617.
PubMed=10692424; DOI=10.1074/jbc.275.9.6276;
de Vet E.C.J.M., Hilkes Y.H.A., Fraaije M.W., van den Bosch H.;
"Alkyl-dihydroxyacetonephosphate synthase. Presence and role of flavin
adenine dinucleotide.";
J. Biol. Chem. 275:6276-6283(2000).
[3]
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, AND MUTAGENESIS OF
THR-309; ARG-419; LEU-469; ARG-515 AND TYR-578.
PubMed=23112191; DOI=10.1073/pnas.1215128109;
Nenci S., Piano V., Rosati S., Aliverti A., Pandini V., Fraaije M.W.,
Heck A.J., Edmondson D.E., Mattevi A.;
"Precursor of ether phospholipids is synthesized by a flavoenzyme
through covalent catalysis.";
Proc. Natl. Acad. Sci. U.S.A. 109:18791-18796(2012).
-!- 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. {ECO:0000269|PubMed:23112191}.
-!- CATALYTIC ACTIVITY: 1-acyl-glycerone 3-phosphate + a long-chain
alcohol = an alkyl-glycerone 3-phosphate + a long-chain acid
anion. {ECO:0000269|PubMed:23112191}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:23112191};
-!- PATHWAY: Glycerolipid metabolism; ether lipid biosynthesis.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23112191}.
-!- SUBCELLULAR LOCATION: Peroxisome.
-!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase
type 4 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y08826; CAA70060.1; -; mRNA.
RefSeq; XP_005007711.2; XM_005007654.2.
PDB; 4BBY; X-ray; 1.90 A; A/B/C/D=1-658.
PDB; 4BC7; X-ray; 2.40 A; A/B/C/D=1-658.
PDB; 4BC9; X-ray; 2.41 A; A/B/C/D=1-658.
PDB; 4BCA; X-ray; 2.40 A; A/B/C/D=1-658.
PDB; 5ADZ; X-ray; 2.20 A; A/B/C/D=1-658.
PDB; 5AE1; X-ray; 2.10 A; A/B/C/D=1-658.
PDB; 5AE2; X-ray; 2.00 A; A/B/C/D=1-658.
PDB; 5AE3; X-ray; 2.18 A; A/B/C/D=1-658.
PDBsum; 4BBY; -.
PDBsum; 4BC7; -.
PDBsum; 4BC9; -.
PDBsum; 4BCA; -.
PDBsum; 5ADZ; -.
PDBsum; 5AE1; -.
PDBsum; 5AE2; -.
PDBsum; 5AE3; -.
ProteinModelPortal; P97275; -.
SMR; P97275; -.
STRING; 10141.ENSCPOP00000000601; -.
SwissLipids; SLP:000000212; -.
Ensembl; ENSCPOT00000000684; ENSCPOP00000000601; ENSCPOG00000000679.
GeneID; 100734021; -.
CTD; 8540; -.
eggNOG; KOG1233; Eukaryota.
eggNOG; COG0277; LUCA.
GeneTree; ENSGT00530000063515; -.
HOGENOM; HOG000231620; -.
HOVERGEN; HBG004179; -.
InParanoid; P97275; -.
OMA; AFPNFEQ; -.
OrthoDB; EOG091G07KJ; -.
TreeFam; TF313830; -.
SABIO-RK; P97275; -.
UniPathway; UPA00781; -.
Proteomes; UP000005447; Unassembled WGS sequence.
Bgee; ENSCPOG00000000679; -.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IEA:Ensembl.
GO; GO:0005778; C:peroxisomal membrane; IEA:Ensembl.
GO; GO:0008609; F:alkylglycerone-phosphate synthase activity; IDA:UniProtKB.
GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
GO; GO:0008611; P:ether lipid biosynthetic process; IDA:UniProtKB.
Gene3D; 1.10.45.10; -; 1.
Gene3D; 3.30.43.10; -; 1.
Gene3D; 3.30.465.10; -; 1.
InterPro; IPR025650; Alkyl-DHAP_Synthase.
InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2.
InterPro; IPR016166; FAD-bd_2.
InterPro; IPR036318; FAD-bd_2-like_sf.
InterPro; IPR016167; FAD-bd_2_sub1.
InterPro; IPR016164; FAD-linked_Oxase-like_C.
InterPro; IPR004113; FAD-linked_oxidase_C.
InterPro; IPR006094; Oxid_FAD_bind_N.
InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
PANTHER; PTHR11748:SF3; PTHR11748:SF3; 1.
Pfam; PF02913; FAD-oxidase_C; 1.
Pfam; PF01565; FAD_binding_4; 1.
SUPFAM; SSF55103; SSF55103; 2.
SUPFAM; SSF56176; SSF56176; 1.
PROSITE; PS51387; FAD_PCMH; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; FAD; Flavoprotein; Lipid biosynthesis;
Lipid metabolism; Peroxisome; Phosphoprotein; Reference proteome;
Transferase; Transit peptide.
TRANSIT 1 58 Peroxisome. {ECO:0000269|PubMed:8995366}.
CHAIN 59 658 Alkyldihydroxyacetonephosphate synthase,
peroxisomal.
/FTId=PRO_0000020430.
DOMAIN 202 384 FAD-binding PCMH-type.
{ECO:0000255|PROSITE-ProRule:PRU00718}.
NP_BIND 234 240 FAD. {ECO:0000269|PubMed:23112191}.
NP_BIND 303 309 FAD. {ECO:0000269|PubMed:23112191}.
NP_BIND 316 319 FAD. {ECO:0000269|PubMed:23112191}.
NP_BIND 368 374 FAD. {ECO:0000269|PubMed:23112191}.
REGION 615 617 Important for enzyme activity.
COMPBIAS 2 14 Poly-Ala.
ACT_SITE 578 578 Proton donor/acceptor.
{ECO:0000269|PubMed:23112191}.
BINDING 515 515 Substrate.
SITE 419 419 Important for enzyme activity.
MOD_RES 65 65 Phosphoserine.
{ECO:0000250|UniProtKB:O00116}.
MOD_RES 74 74 Phosphothreonine.
{ECO:0000250|UniProtKB:O00116}.
MOD_RES 102 102 N6-acetyllysine.
{ECO:0000250|UniProtKB:O00116}.
MOD_RES 347 347 N6-acetyllysine.
{ECO:0000250|UniProtKB:O00116}.
MUTAGEN 300 300 H->A: Loss of activity.
{ECO:0000269|PubMed:10692424}.
MUTAGEN 309 309 T->I: Impaired FAD binding and protein
stability. Loss of activity.
{ECO:0000269|PubMed:23112191}.
MUTAGEN 367 367 S->A: Strongly reduced activity.
{ECO:0000269|PubMed:10692424}.
MUTAGEN 419 419 R->H: Loss of activity.
{ECO:0000269|PubMed:10692424,
ECO:0000269|PubMed:23112191}.
MUTAGEN 419 419 R->K: Strongly reduced activity.
{ECO:0000269|PubMed:10692424,
ECO:0000269|PubMed:23112191}.
MUTAGEN 469 469 L->P: Impaired FAD binding and protein
stability. Loss of activity.
{ECO:0000269|PubMed:23112191}.
MUTAGEN 515 515 R->L: Impaired FAD binding and protein
stability. Loss of activity.
{ECO:0000269|PubMed:23112191}.
MUTAGEN 578 578 Y->F: Loss of activity.
{ECO:0000269|PubMed:23112191}.
MUTAGEN 615 615 H->A: Loss of activity.
{ECO:0000269|PubMed:10692424}.
MUTAGEN 616 616 H->A: Loss of activity.
{ECO:0000269|PubMed:10692424}.
MUTAGEN 617 617 H->A: Loss of activity.
{ECO:0000269|PubMed:10692424}.
HELIX 87 89 {ECO:0000244|PDB:4BBY}.
STRAND 95 98 {ECO:0000244|PDB:4BBY}.
STRAND 103 105 {ECO:0000244|PDB:4BBY}.
STRAND 111 113 {ECO:0000244|PDB:4BBY}.
STRAND 115 118 {ECO:0000244|PDB:4BBY}.
TURN 119 122 {ECO:0000244|PDB:4BC9}.
HELIX 128 136 {ECO:0000244|PDB:4BBY}.
STRAND 140 142 {ECO:0000244|PDB:5AE2}.
HELIX 152 154 {ECO:0000244|PDB:5AE1}.
HELIX 162 171 {ECO:0000244|PDB:4BBY}.
STRAND 174 176 {ECO:0000244|PDB:4BBY}.
HELIX 179 184 {ECO:0000244|PDB:4BBY}.
HELIX 191 198 {ECO:0000244|PDB:4BBY}.
STRAND 207 211 {ECO:0000244|PDB:4BBY}.
HELIX 215 227 {ECO:0000244|PDB:4BBY}.
STRAND 231 237 {ECO:0000244|PDB:4BBY}.
STRAND 241 243 {ECO:0000244|PDB:4BBY}.
STRAND 255 259 {ECO:0000244|PDB:4BBY}.
STRAND 266 270 {ECO:0000244|PDB:4BBY}.
TURN 271 274 {ECO:0000244|PDB:4BBY}.
STRAND 275 279 {ECO:0000244|PDB:4BBY}.
HELIX 284 293 {ECO:0000244|PDB:4BBY}.
TURN 303 307 {ECO:0000244|PDB:4BBY}.
HELIX 310 316 {ECO:0000244|PDB:4BBY}.
HELIX 323 326 {ECO:0000244|PDB:4BBY}.
HELIX 329 332 {ECO:0000244|PDB:4BBY}.
STRAND 333 340 {ECO:0000244|PDB:4BBY}.
STRAND 343 346 {ECO:0000244|PDB:4BBY}.
STRAND 356 358 {ECO:0000244|PDB:4BBY}.
HELIX 361 364 {ECO:0000244|PDB:4BBY}.
STRAND 373 380 {ECO:0000244|PDB:4BBY}.
STRAND 386 397 {ECO:0000244|PDB:4BBY}.
HELIX 398 410 {ECO:0000244|PDB:4BBY}.
STRAND 416 421 {ECO:0000244|PDB:4BBY}.
HELIX 423 431 {ECO:0000244|PDB:4BBY}.
STRAND 432 434 {ECO:0000244|PDB:4BCA}.
HELIX 444 449 {ECO:0000244|PDB:5AE2}.
TURN 451 457 {ECO:0000244|PDB:5ADZ}.
TURN 460 462 {ECO:0000244|PDB:4BBY}.
STRAND 464 472 {ECO:0000244|PDB:4BBY}.
HELIX 474 489 {ECO:0000244|PDB:4BBY}.
TURN 490 492 {ECO:0000244|PDB:4BBY}.
HELIX 498 520 {ECO:0000244|PDB:4BBY}.
STRAND 523 533 {ECO:0000244|PDB:4BBY}.
HELIX 534 536 {ECO:0000244|PDB:4BBY}.
HELIX 537 554 {ECO:0000244|PDB:4BBY}.
STRAND 562 570 {ECO:0000244|PDB:4BBY}.
STRAND 572 584 {ECO:0000244|PDB:4BBY}.
HELIX 591 608 {ECO:0000244|PDB:4BBY}.
STRAND 615 617 {ECO:0000244|PDB:4BBY}.
TURN 620 622 {ECO:0000244|PDB:4BBY}.
HELIX 624 626 {ECO:0000244|PDB:4BBY}.
HELIX 627 631 {ECO:0000244|PDB:4BBY}.
HELIX 633 646 {ECO:0000244|PDB:4BBY}.
SEQUENCE 658 AA; 72846 MW; B6272EB407EBB5F1 CRC64;
MAEAAAAAAA AAAAGETSAS SGSAAERDPD QDRAGRRLRV LSGHLLGRPQ EALSTNECKA
RRAASAATAA PTATPAAPES GIIPKKRQEL MKWNGWGYND SKFFLNKKGQ LELTGKRYPL
SGVALPTFKD WIQNTFGINL DHKTTSKASL NPSDTPPSIV NEDFLHELKK TNISYSQEAD
DRVFRAHGHC LHEIFLLREG MFERIPDIVL WPTCHDDVVK IVNLACKYNL CIIPIGGGTS
VSYGLMCPAD ETRTIISLDT SQMNRILWVD ENNLTAHVEA GITGQELERQ LKESGYCTGH
EPDSLEFSTV GGWISTRASG MKKNIYGNIE DLVVHMKVVT PRGVIEKSCQ GPRMSTGPDI
HHFIMGSEGT LGVITEATIK IRPTPEYQKY GSVAFPNFEQ GVACLREIAK QRCAPASIRL
MDNQQFQFGH ALKPQVSSIF TSFLDGLKKF YITKFKGFDP NQLSVATLLF EGDREKVLQH
EKQVYDIAAK FGGLAAGEDN GQRGYLLTYV IAYMRDLGLE YYIIGESFET SAPWDRVVDL
CRNVKERIRR ECKEKGVQFP PLSTCRVTQT YDAGACIYFY FAFNYRGISD PLAVFEQTEA
AAREEILANG GSLSHHHGVG KLRKQWLKES ISDVGFGMLK SVKDYVDPTN IFGNRNLL


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