Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

NAD(P)H-dependent D-xylose reductase I,II

Gene

xyrA

Organism
Candida tropicalis (Yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Reduces D-xylose into xylitol. Has a preference for NADPH, but can also utilize NADH as cosubstrate (By similarity).By similarity

Catalytic activityi

Xylitol + NAD(P)+ = D-xylose + NAD(P)H.

Pathwayi: D-xylose degradation

This protein is involved in the pathway D-xylose degradation, which is part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the pathway D-xylose degradation and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei54 – 541Proton donorBy similarity
Sitei83 – 831Lowers pKa of active site TyrBy similarity
Binding sitei116 – 1161SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi171 – 1722NAD or NADPBy similarity
Nucleotide bindingi220 – 22910NAD or NADPBy similarity
Nucleotide bindingi276 – 28611NAD or NADPBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Carbohydrate metabolism, Xylose metabolism

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

UniPathwayiUPA00810.

Names & Taxonomyi

Protein namesi
Recommended name:
NAD(P)H-dependent D-xylose reductase I,II (EC:1.1.1.307)
Short name:
XR
Gene namesi
Name:xyrA
OrganismiCandida tropicalis (Yeast)
Taxonomic identifieri5482 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 324324NAD(P)H-dependent D-xylose reductase I,IIPRO_0000124662Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi294747.XP_002546515.1.

Structurei

3D structure databases

ProteinModelPortaliO13283.
SMRiO13283. Positions 6-324.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

eggNOGiKOG1577. Eukaryota.
COG0656. LUCA.

Family and domain databases

CDDicd06660. Aldo_ket_red. 1 hit.
Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red/Kv-b.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 2 hits.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O13283-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTTPTIPTI KLNSGYEMPL VGFGCWKVTN ATAADQIYNA IKTGYRLFDG
60 70 80 90 100
AEDYGNEKEV GEGINRAIKE GLVKREELFI TSKLWNNFHD PKNVETALNK
110 120 130 140 150
TLSDLNLDYV DLFLIHFPIA FKFVPIEEKY PPGFYCGDGD NFHYEDVPLL
160 170 180 190 200
DTWKALEKLV EAGKIKSIGI SNFTGALIYD LIRGATIKPA VLQIEHHPYL
210 220 230 240 250
QQPKLIEYVQ KAGIAITGYS SFGPQSFLEL ESKRALNTPT LFEHETIKLI
260 270 280 290 300
ADKHGKSPAQ VLLRWATQRN IAVIPKSNNP ERLAQNLSVV DFDLTKDDLD
310 320
NIAKLDIGLR FNDPWDWDNI PIFV
Length:324
Mass (Da):36,575
Last modified:January 1, 1998 - v1
Checksum:i3002FFBDA21FA3E0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB002105 Genomic DNA. Translation: BAA19476.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB002105 Genomic DNA. Translation: BAA19476.1.

3D structure databases

ProteinModelPortaliO13283.
SMRiO13283. Positions 6-324.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi294747.XP_002546515.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1577. Eukaryota.
COG0656. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00810.

Family and domain databases

CDDicd06660. Aldo_ket_red. 1 hit.
Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red/Kv-b.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 2 hits.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiXYL1_CANTR
AccessioniPrimary (citable) accession number: O13283
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: January 1, 1998
Last modified: September 7, 2016
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.