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Protein

Alkyldihydroxyacetonephosphate synthase, peroxisomal

Gene

AGPS

Organism
Cavia porcellus (Guinea pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Cofactori

FAD1 Publication

Pathwayi: ether lipid biosynthesis

This protein is involved in the pathway ether lipid biosynthesis, which is part of Glycerolipid metabolism.
View all proteins of this organism that are known to be involved in the pathway ether lipid biosynthesis and in Glycerolipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei419Important for enzyme activity1
Binding sitei515Substrate1
Active sitei578Proton donor/acceptor1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi234 – 240FAD1 Publication7
Nucleotide bindingi303 – 309FAD1 Publication7
Nucleotide bindingi316 – 319FAD1 Publication4
Nucleotide bindingi368 – 374FAD1 Publication7

GO - Molecular functioni

  • alkylglycerone-phosphate synthase activity Source: UniProtKB
  • FAD binding Source: UniProtKB
  • oxidoreductase activity, acting on CH-OH group of donors Source: InterPro

GO - Biological processi

  • ether lipid biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

SABIO-RKP97275.
UniPathwayiUPA00781.

Chemistry databases

SwissLipidsiSLP:000000212.

Names & Taxonomyi

Protein namesi
Recommended name:
Alkyldihydroxyacetonephosphate synthase, peroxisomal (EC:2.5.1.26)
Short name:
Alkyl-DHAP synthase
Alternative name(s):
Alkylglycerone-phosphate synthase
Gene namesi
Name:AGPS
OrganismiCavia porcellus (Guinea pig)
Taxonomic identifieri10141 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia
Proteomesi
  • UP000005447 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi300H → A: Loss of activity. 1 Publication1
Mutagenesisi309T → I: Impaired FAD binding and protein stability. Loss of activity. 1 Publication1
Mutagenesisi367S → A: Strongly reduced activity. 1 Publication1
Mutagenesisi419R → H: Loss of activity. 2 Publications1
Mutagenesisi419R → K: Strongly reduced activity. 2 Publications1
Mutagenesisi469L → P: Impaired FAD binding and protein stability. Loss of activity. 1 Publication1
Mutagenesisi515R → L: Impaired FAD binding and protein stability. Loss of activity. 1 Publication1
Mutagenesisi578Y → F: Loss of activity. 1 Publication1
Mutagenesisi615H → A: Loss of activity. 1 Publication1
Mutagenesisi616H → A: Loss of activity. 1 Publication1
Mutagenesisi617H → A: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 58Peroxisome1 PublicationAdd BLAST58
ChainiPRO_000002043059 – 658Alkyldihydroxyacetonephosphate synthase, peroxisomalAdd BLAST600

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei65PhosphoserineBy similarity1
Modified residuei74PhosphothreonineBy similarity1
Modified residuei102N6-acetyllysineBy similarity1
Modified residuei347N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi10141.ENSCPOP00000000601.

Structurei

Secondary structure

1658
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi87 – 89Combined sources3
Beta strandi95 – 98Combined sources4
Beta strandi103 – 105Combined sources3
Beta strandi111 – 113Combined sources3
Beta strandi115 – 118Combined sources4
Turni119 – 122Combined sources4
Helixi128 – 136Combined sources9
Beta strandi140 – 142Combined sources3
Helixi152 – 154Combined sources3
Helixi162 – 171Combined sources10
Beta strandi174 – 176Combined sources3
Helixi179 – 184Combined sources6
Helixi191 – 198Combined sources8
Beta strandi207 – 211Combined sources5
Helixi215 – 227Combined sources13
Beta strandi231 – 237Combined sources7
Beta strandi241 – 243Combined sources3
Beta strandi255 – 259Combined sources5
Beta strandi266 – 270Combined sources5
Turni271 – 274Combined sources4
Beta strandi275 – 279Combined sources5
Helixi284 – 293Combined sources10
Turni303 – 307Combined sources5
Helixi310 – 316Combined sources7
Helixi323 – 326Combined sources4
Helixi329 – 332Combined sources4
Beta strandi333 – 340Combined sources8
Beta strandi343 – 346Combined sources4
Beta strandi356 – 358Combined sources3
Helixi361 – 364Combined sources4
Beta strandi373 – 380Combined sources8
Beta strandi386 – 397Combined sources12
Helixi398 – 410Combined sources13
Beta strandi416 – 421Combined sources6
Helixi423 – 431Combined sources9
Beta strandi432 – 434Combined sources3
Helixi444 – 449Combined sources6
Turni451 – 457Combined sources7
Turni460 – 462Combined sources3
Beta strandi464 – 472Combined sources9
Helixi474 – 489Combined sources16
Turni490 – 492Combined sources3
Helixi498 – 520Combined sources23
Beta strandi523 – 533Combined sources11
Helixi534 – 536Combined sources3
Helixi537 – 554Combined sources18
Beta strandi562 – 570Combined sources9
Beta strandi572 – 584Combined sources13
Helixi591 – 608Combined sources18
Beta strandi615 – 617Combined sources3
Turni620 – 622Combined sources3
Helixi624 – 626Combined sources3
Helixi627 – 631Combined sources5
Helixi633 – 646Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5ADZX-ray2.20A/B/C/D1-658[»]
5AE1X-ray2.10A/B/C/D1-658[»]
5AE2X-ray2.00A/B/C/D1-658[»]
5AE3X-ray2.18A/B/C/D1-658[»]
ProteinModelPortaliP97275.
SMRiP97275.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini202 – 384FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST183

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni615 – 617Important for enzyme activity3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2 – 14Poly-AlaAdd BLAST13

Sequence similaritiesi

Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1233. Eukaryota.
COG0277. LUCA.
GeneTreeiENSGT00530000063515.
HOGENOMiHOG000231620.
HOVERGENiHBG004179.
InParanoidiP97275.
OMAiEIMKWNG.
OrthoDBiEOG091G07KJ.
TreeFamiTF313830.

Family and domain databases

Gene3Di3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProiIPR025650. 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]
PANTHERiPTHR11748:SF3. PTHR11748:SF3. 1 hit.
PfamiPF02913. FAD-oxidase_C. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMiSSF55103. SSF55103. 2 hits.
SSF56176. SSF56176. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P97275-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEAAAAAAA AAAAGETSAS SGSAAERDPD QDRAGRRLRV LSGHLLGRPQ
60 70 80 90 100
EALSTNECKA RRAASAATAA PTATPAAPES GIIPKKRQEL MKWNGWGYND
110 120 130 140 150
SKFFLNKKGQ LELTGKRYPL SGVALPTFKD WIQNTFGINL DHKTTSKASL
160 170 180 190 200
NPSDTPPSIV NEDFLHELKK TNISYSQEAD DRVFRAHGHC LHEIFLLREG
210 220 230 240 250
MFERIPDIVL WPTCHDDVVK IVNLACKYNL CIIPIGGGTS VSYGLMCPAD
260 270 280 290 300
ETRTIISLDT SQMNRILWVD ENNLTAHVEA GITGQELERQ LKESGYCTGH
310 320 330 340 350
EPDSLEFSTV GGWISTRASG MKKNIYGNIE DLVVHMKVVT PRGVIEKSCQ
360 370 380 390 400
GPRMSTGPDI HHFIMGSEGT LGVITEATIK IRPTPEYQKY GSVAFPNFEQ
410 420 430 440 450
GVACLREIAK QRCAPASIRL MDNQQFQFGH ALKPQVSSIF TSFLDGLKKF
460 470 480 490 500
YITKFKGFDP NQLSVATLLF EGDREKVLQH EKQVYDIAAK FGGLAAGEDN
510 520 530 540 550
GQRGYLLTYV IAYMRDLGLE YYIIGESFET SAPWDRVVDL CRNVKERIRR
560 570 580 590 600
ECKEKGVQFP PLSTCRVTQT YDAGACIYFY FAFNYRGISD PLAVFEQTEA
610 620 630 640 650
AAREEILANG GSLSHHHGVG KLRKQWLKES ISDVGFGMLK SVKDYVDPTN

IFGNRNLL
Length:658
Mass (Da):72,846
Last modified:May 1, 1997 - v1
Checksum:iB6272EB407EBB5F1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08826 mRNA. Translation: CAA70060.1.
RefSeqiXP_005007711.2. XM_005007654.2.

Genome annotation databases

EnsembliENSCPOT00000000684; ENSCPOP00000000601; ENSCPOG00000000679.
GeneIDi100734021.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08826 mRNA. Translation: CAA70060.1.
RefSeqiXP_005007711.2. XM_005007654.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5ADZX-ray2.20A/B/C/D1-658[»]
5AE1X-ray2.10A/B/C/D1-658[»]
5AE2X-ray2.00A/B/C/D1-658[»]
5AE3X-ray2.18A/B/C/D1-658[»]
ProteinModelPortaliP97275.
SMRiP97275.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10141.ENSCPOP00000000601.

Chemistry databases

SwissLipidsiSLP:000000212.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSCPOT00000000684; ENSCPOP00000000601; ENSCPOG00000000679.
GeneIDi100734021.

Organism-specific databases

CTDi8540.

Phylogenomic databases

eggNOGiKOG1233. Eukaryota.
COG0277. LUCA.
GeneTreeiENSGT00530000063515.
HOGENOMiHOG000231620.
HOVERGENiHBG004179.
InParanoidiP97275.
OMAiEIMKWNG.
OrthoDBiEOG091G07KJ.
TreeFamiTF313830.

Enzyme and pathway databases

UniPathwayiUPA00781.
SABIO-RKP97275.

Family and domain databases

Gene3Di3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProiIPR025650. 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]
PANTHERiPTHR11748:SF3. PTHR11748:SF3. 1 hit.
PfamiPF02913. FAD-oxidase_C. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMiSSF55103. SSF55103. 2 hits.
SSF56176. SSF56176. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiADAS_CAVPO
AccessioniPrimary (citable) accession number: P97275
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: November 2, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.