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Protein

Peroxisomal hydratase-dehydrogenase-epimerase

Gene
N/A
Organism
Candida tropicalis (Yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Second trifunctional enzyme acting on the beta-oxidation pathway for fatty acids, possessing hydratase-dehydrogenase-epimerase activities. Converts trans-2-enoyl-CoA via D-3-hydroxyacyl-CoA to 3-ketoacyl-CoA.

Catalytic activityi

(3R)-3-hydroxyacyl-CoA = (2E)-2-enoyl-CoA + H2O.
(R)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.

Pathwayi: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei20NAD; via amide nitrogenBy similarity1
Binding sitei39NADBy similarity1
Binding sitei98NAD; via carbonyl oxygenBy similarity1
Binding sitei150SubstrateBy similarity1
Active sitei163Proton acceptorPROSITE-ProRule annotation1
Binding sitei454Substrate1 Publication1
Active sitei467Proton acceptorPROSITE-ProRule annotation1
Binding sitei729(3R)-3-hydroxydecanoyl-CoA1
Binding sitei831(3R)-3-hydroxydecanoyl-CoA; via amide nitrogen1
Binding sitei856(3R)-3-hydroxydecanoyl-CoA; via carbonyl oxygen1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi12 – 36NADBy similarityAdd BLAST25
Nucleotide bindingi74 – 75NADBy similarity2
Nucleotide bindingi163 – 167NADBy similarity5
Nucleotide bindingi195 – 198NADBy similarity4
Nucleotide bindingi326 – 350NADAdd BLAST25

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase, Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BRENDAi4.2.1.119. 1146.
UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal hydratase-dehydrogenase-epimerase
Short name:
HDE
Alternative name(s):
Multifunctional beta-oxidation protein
Short name:
MFP
Including the following 2 domains:
2-enoyl-CoA hydratase (EC:4.2.1.119)
(3R)-3-hydroxyacyl-CoA dehydrogenase (EC:1.1.1.n12)
OrganismiCandida tropicalis (Yeast)
Taxonomic identifieri5482 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000546981 – 906Peroxisomal hydratase-dehydrogenase-epimeraseAdd BLAST906

Proteomic databases

PRIDEiP22414.

Expressioni

Inductioni

By growth on N-alkanes or fatty acids.

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1906
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 13Combined sources4
Turni14 – 17Combined sources4
Helixi19 – 30Combined sources12
Beta strandi34 – 38Combined sources5
Helixi53 – 63Combined sources11
Beta strandi67 – 71Combined sources5
Helixi78 – 89Combined sources12
Beta strandi94 – 97Combined sources4
Turni107 – 109Combined sources3
Helixi112 – 122Combined sources11
Helixi124 – 140Combined sources17
Beta strandi143 – 148Combined sources6
Helixi151 – 155Combined sources5
Helixi161 – 181Combined sources21
Helixi182 – 184Combined sources3
Beta strandi186 – 193Combined sources8
Helixi198 – 201Combined sources4
Helixi206 – 209Combined sources4
Helixi214 – 224Combined sources11
Beta strandi226 – 228Combined sources3
Beta strandi235 – 239Combined sources5
Beta strandi242 – 250Combined sources9
Helixi264 – 274Combined sources11
Helixi284 – 286Combined sources3
Beta strandi292 – 294Combined sources3
Helixi297 – 304Combined sources8
Beta strandi324 – 329Combined sources6
Helixi333 – 344Combined sources12
Beta strandi348 – 352Combined sources5
Helixi358 – 366Combined sources9
Beta strandi370 – 374Combined sources5
Helixi378 – 393Combined sources16
Beta strandi398 – 401Combined sources4
Turni411 – 413Combined sources3
Helixi416 – 426Combined sources11
Helixi428 – 443Combined sources16
Beta strandi447 – 452Combined sources6
Helixi455 – 458Combined sources4
Helixi465 – 485Combined sources21
Helixi486 – 488Combined sources3
Beta strandi490 – 497Combined sources8
Helixi518 – 520Combined sources3
Helixi522 – 527Combined sources6
Beta strandi539 – 543Combined sources5
Beta strandi546 – 554Combined sources9
Beta strandi562 – 564Combined sources3
Helixi567 – 577Combined sources11
Beta strandi581 – 583Combined sources3
Helixi590 – 602Combined sources13
Beta strandi632 – 635Combined sources4
Helixi637 – 646Combined sources10
Helixi651 – 653Combined sources3
Helixi654 – 657Combined sources4
Helixi668 – 675Combined sources8
Helixi679 – 682Combined sources4
Turni683 – 687Combined sources5
Beta strandi688 – 691Combined sources4
Helixi694 – 696Combined sources3
Beta strandi697 – 706Combined sources10
Beta strandi708 – 710Combined sources3
Beta strandi713 – 729Combined sources17
Beta strandi732 – 743Combined sources12
Turni744 – 746Combined sources3
Beta strandi749 – 759Combined sources11
Helixi774 – 777Combined sources4
Beta strandi788 – 794Combined sources7
Helixi799 – 803Combined sources5
Helixi804 – 806Combined sources3
Helixi811 – 813Combined sources3
Helixi816 – 821Combined sources6
Helixi831 – 846Combined sources16
Beta strandi849 – 856Combined sources8
Beta strandi865 – 872Combined sources8
Beta strandi874 – 884Combined sources11
Turni885 – 888Combined sources4
Beta strandi889 – 899Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PN2X-ray1.95A/B/C/D627-906[»]
1PN4X-ray2.35A/B/C/D627-906[»]
2ET6X-ray2.22A1-604[»]
ProteinModelPortaliP22414.
SMRiP22414.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22414.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini782 – 893MaoC-likeAdd BLAST112

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni5 – 228Short-chain dehydrogenase like 1Add BLAST224
Regioni319 – 532Short-chain dehydrogenase like 2Add BLAST214
Regioni699 – 700(3R)-3-hydroxydecanoyl-CoA binding2
Regioni808 – 813(3R)-3-hydroxydecanoyl-CoA binding6

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi904 – 906Microbody targeting signalSequence analysis3

Domaini

Contains two SDR domains.

Sequence similaritiesi

Contains 1 MaoC-like domain.Curated

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di3.10.129.10. 2 hits.
3.40.50.720. 2 hits.
InterProiIPR029069. HotDog_dom.
IPR002539. MaoC_dom.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PfamiPF00106. adh_short. 2 hits.
PF01575. MaoC_dehydratas. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 2 hits.
SSF54637. SSF54637. 2 hits.
PROSITEiPS00061. ADH_SHORT. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P22414-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPVDFKDKV VIITGAGGGL GKYYSLEFAK LGAKVVVNDL GGALNGQGGN
60 70 80 90 100
SKAADVVVDE IVKNGGVAVA DYNNVLDGDK IVETAVKNFG TVHVIINNAG
110 120 130 140 150
ILRDASMKKM TEKDYKLVID VHLNGAFAVT KAAWPYFQKQ KYGRIVNTSS
160 170 180 190 200
PAGLYGNFGQ ANYASAKSAL LGFAETLAKE GAKYNIKANA IAPLARSRMT
210 220 230 240 250
ESILPPPMLE KLGPEKVAPL VLYLSSAENE LTGQFFEVAA GFYAQIRWER
260 270 280 290 300
SGGVLFKPDQ SFTAEVVAKR FSEILDYDDS RKPEYLKNQY PFMLNDYATL
310 320 330 340 350
TNEARKLPAN DASGAPTVSL KDKVVLITGA GAGLGKEYAK WFAKYGAKVV
360 370 380 390 400
VNDFKDATKT VDEIKAAGGE AWPDQHDVAK DSEAIIKNVI DKYGTIDILV
410 420 430 440 450
NNAGILRDRS FAKMSKQEWD SVQQVHLIGT FNLSRLAWPY FVEKQFGRII
460 470 480 490 500
NITSTSGIYG NFGQANYSSS KAGILGLSKT MAIEGAKNNI KVNIVAPHAE
510 520 530 540 550
TAMTLTIFRE QDKNLYHADQ VAPLLVYLGT DDVPVTGETF EIGGGWIGNT
560 570 580 590 600
RWQRAKGAVS HDEHTTVEFI KEHLNEITDF TTDTENPKST TESSMAILSA
610 620 630 640 650
VGGDDDDDDE DEEEDEGDEE EDEEDEEEDD PVWRFDDRDV ILYNIALGAT
660 670 680 690 700
TKQLKYVYEN DSDFQVIPTF GHLITFNSGK SQNSFAKLLR NFNPMLLLHG
710 720 730 740 750
EHYLKVHSWP PPTEGEIKTT FEPIATTPKG TNVVIVHGSK SVDNKSGELI
760 770 780 790 800
YSNEATYFIR NCQADNKVYA DRPAFATNQF LAPKRAPDYQ VDVPVSEDLA
810 820 830 840 850
ALYRLSGDRN PLHIDPNFAK GAKFPKPILH GMCTYGLSAK ALIDKFGMFN
860 870 880 890 900
EIKARFTGIV FPGETLRVLA WKESDDTIVF QTHVVDRGTI AINNAAIKLV

GDKAKI
Length:906
Mass (Da):99,469
Last modified:October 1, 1996 - v2
Checksum:i65AB88C8671C967B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti540F → S in AAA62847 (PubMed:3267241).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22765 mRNA. Translation: AAA62847.1.
X57854 Genomic DNA. Translation: CAA40989.1.
PIRiS32607.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22765 mRNA. Translation: AAA62847.1.
X57854 Genomic DNA. Translation: CAA40989.1.
PIRiS32607.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PN2X-ray1.95A/B/C/D627-906[»]
1PN4X-ray2.35A/B/C/D627-906[»]
2ET6X-ray2.22A1-604[»]
ProteinModelPortaliP22414.
SMRiP22414.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP22414.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00659.
BRENDAi4.2.1.119. 1146.

Miscellaneous databases

EvolutionaryTraceiP22414.

Family and domain databases

Gene3Di3.10.129.10. 2 hits.
3.40.50.720. 2 hits.
InterProiIPR029069. HotDog_dom.
IPR002539. MaoC_dom.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PfamiPF00106. adh_short. 2 hits.
PF01575. MaoC_dehydratas. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 2 hits.
SSF54637. SSF54637. 2 hits.
PROSITEiPS00061. ADH_SHORT. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFOX2_CANTR
AccessioniPrimary (citable) accession number: P22414
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Multifunctional enzyme

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.