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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei20 – 201NAD; via amide nitrogenBy similarity
Binding sitei39 – 391NADBy similarity
Binding sitei98 – 981NAD; via carbonyl oxygenBy similarity
Binding sitei150 – 1501SubstrateBy similarity
Active sitei163 – 1631Proton acceptorPROSITE-ProRule annotation
Binding sitei454 – 4541Substrate1 Publication
Active sitei467 – 4671Proton acceptorPROSITE-ProRule annotation
Binding sitei729 – 7291(3R)-3-hydroxydecanoyl-CoA
Binding sitei831 – 8311(3R)-3-hydroxydecanoyl-CoA; via amide nitrogen
Binding sitei856 – 8561(3R)-3-hydroxydecanoyl-CoA; via carbonyl oxygen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 3625NADBy similarityAdd
BLAST
Nucleotide bindingi74 – 752NADBy similarity
Nucleotide bindingi163 – 1675NADBy similarity
Nucleotide bindingi195 – 1984NADBy similarity
Nucleotide bindingi326 – 35025NADAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 906906Peroxisomal hydratase-dehydrogenase-epimerasePRO_0000054698Add
BLAST

Expressioni

Inductioni

By growth on N-alkanes or fatty acids.

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
906
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 134Combined sources
Turni14 – 174Combined sources
Helixi19 – 3012Combined sources
Beta strandi34 – 385Combined sources
Helixi53 – 6311Combined sources
Beta strandi67 – 715Combined sources
Helixi78 – 8912Combined sources
Beta strandi94 – 974Combined sources
Turni107 – 1093Combined sources
Helixi112 – 12211Combined sources
Helixi124 – 14017Combined sources
Beta strandi143 – 1486Combined sources
Helixi151 – 1555Combined sources
Helixi161 – 18121Combined sources
Helixi182 – 1843Combined sources
Beta strandi186 – 1938Combined sources
Helixi198 – 2014Combined sources
Helixi206 – 2094Combined sources
Helixi214 – 22411Combined sources
Beta strandi226 – 2283Combined sources
Beta strandi235 – 2395Combined sources
Beta strandi242 – 2509Combined sources
Helixi264 – 27411Combined sources
Helixi284 – 2863Combined sources
Beta strandi292 – 2943Combined sources
Helixi297 – 3048Combined sources
Beta strandi324 – 3296Combined sources
Helixi333 – 34412Combined sources
Beta strandi348 – 3525Combined sources
Helixi358 – 3669Combined sources
Beta strandi370 – 3745Combined sources
Helixi378 – 39316Combined sources
Beta strandi398 – 4014Combined sources
Turni411 – 4133Combined sources
Helixi416 – 42611Combined sources
Helixi428 – 44316Combined sources
Beta strandi447 – 4526Combined sources
Helixi455 – 4584Combined sources
Helixi465 – 48521Combined sources
Helixi486 – 4883Combined sources
Beta strandi490 – 4978Combined sources
Helixi518 – 5203Combined sources
Helixi522 – 5276Combined sources
Beta strandi539 – 5435Combined sources
Beta strandi546 – 5549Combined sources
Beta strandi562 – 5643Combined sources
Helixi567 – 57711Combined sources
Beta strandi581 – 5833Combined sources
Helixi590 – 60213Combined sources
Beta strandi632 – 6354Combined sources
Helixi637 – 64610Combined sources
Helixi651 – 6533Combined sources
Helixi654 – 6574Combined sources
Helixi668 – 6758Combined sources
Helixi679 – 6824Combined sources
Turni683 – 6875Combined sources
Beta strandi688 – 6914Combined sources
Helixi694 – 6963Combined sources
Beta strandi697 – 70610Combined sources
Beta strandi708 – 7103Combined sources
Beta strandi713 – 72917Combined sources
Beta strandi732 – 74312Combined sources
Turni744 – 7463Combined sources
Beta strandi749 – 75911Combined sources
Helixi774 – 7774Combined sources
Beta strandi788 – 7947Combined sources
Helixi799 – 8035Combined sources
Helixi804 – 8063Combined sources
Helixi811 – 8133Combined sources
Helixi816 – 8216Combined sources
Helixi831 – 84616Combined sources
Beta strandi849 – 8568Combined sources
Beta strandi865 – 8728Combined sources
Beta strandi874 – 88411Combined sources
Turni885 – 8884Combined sources
Beta strandi889 – 89911Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PN2X-ray1.95A/B/C/D627-906[»]
1PN4X-ray2.35A/B/C/D627-906[»]
2ET6X-ray2.22A1-604[»]
ProteinModelPortaliP22414.
SMRiP22414. Positions 2-603, 631-902.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22414.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini782 – 893112MaoC-likeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni5 – 228224Short-chain dehydrogenase like 1Add
BLAST
Regioni319 – 532214Short-chain dehydrogenase like 2Add
BLAST
Regioni699 – 7002(3R)-3-hydroxydecanoyl-CoA binding
Regioni808 – 8136(3R)-3-hydroxydecanoyl-CoA binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi904 – 9063Microbody targeting signalSequence analysis

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti540 – 5401F → S in AAA62847 (PubMed:3267241).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1PN2X-ray1.95A/B/C/D627-906[»]
1PN4X-ray2.35A/B/C/D627-906[»]
2ET6X-ray2.22A1-604[»]
ProteinModelPortaliP22414.
SMRiP22414. Positions 2-603, 631-902.
ModBaseiSearch...
MobiDBiSearch...

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...

Publicationsi

  1. "cDNA cloning and primary structure determination of the peroxisomal trifunctional enzyme hydratase-dehydrogenase-epimerase from the yeast Candida tropicalis pK233."
    Nuttley W.M., Aitchison J.D., Rachubinski R.A.
    Gene 69:171-180(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ATCC 20336 / pK233 / NCYC 997.
  2. "Glucose-responsive and oleic acid-responsive elements in the gene encoding the peroxisomal trifunctional enzyme of Candida tropicalis."
    Aitchison J.D., Sloots J.A., Nuttley W.M., Rachubinski R.A.
    Gene 105:129-134(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 20336 / pK233 / NCYC 997.
  3. "A common ancestor for Candida tropicalis and dehydrogenases that synthesize antibiotics and steroids."
    Baker M.E.
    FASEB J. 4:3028-3032(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: SIMILARITY TO SHORT CHAIN DEHYDROGENASES OF N-TERMINAL DOMAIN.
  4. "A two-domain structure of one subunit explains unique features of eukaryotic hydratase 2."
    Koski M.K., Haapalainen A.M., Hiltunen J.K., Glumoff T.
    J. Biol. Chem. 279:24666-24672(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 628-906 OF APOENZYME AND IN COMPLEX WITH SUBSTRATE, REACTION MECHANISM.
  5. "Crystal structure of yeast peroxisomal multifunctional enzyme: structural basis for substrate specificity of (3R)-hydroxyacyl-CoA dehydrogenase units."
    Ylianttila M.S., Pursiainen N.V., Haapalainen A.M., Juffer A.H., Poirier Y., Hiltunen J.K., Glumoff T.
    J. Mol. Biol. 358:1286-1295(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS) OF 1-604.

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: April 13, 2016
This is version 108 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.