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Protein

Alcohol oxidase

Gene

AOD1

Organism
Candida boidinii (Yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of methanol to formaldehyde and hydrogen peroxide, the first step in the methanol utilization pathway of methylotrophic yeasts.1 Publication

Catalytic activityi

A primary alcohol + O2 = an aldehyde + H2O2.

Cofactori

Pathwayi: methane degradation

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei567 – 5671Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi8 – 3932FADBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Methanol utilization

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13165.
BRENDAi1.1.3.13. 1100.
UniPathwayiUPA00147.

Names & Taxonomyi

Protein namesi
Recommended name:
Alcohol oxidase (EC:1.1.3.13)
Short name:
AO
Short name:
AOX
Alternative name(s):
Methanol oxidase
Short name:
MOX
Gene namesi
Name:AOD1
OrganismiCandida boidinii (Yeast)
Taxonomic identifieri5477 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesPichiaceaeOgataeaOgataea/Candida clade

Subcellular locationi

  • Peroxisome matrix 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 663662Alcohol oxidasePRO_0000205580Add
BLAST

Expressioni

Inductioni

Induced by methanol. Subject to strong carbon catabolite repression (By similarity).By similarity

Interactioni

Subunit structurei

Homooctamer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ00922.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi661 – 6633Microbody targeting signalSequence analysis

Domaini

The C-terminal peroxisomal targeting signal (PTS) is essential for the efficient targeting and import of AOX into peroxisomes via the PTS1 pathway.By similarity

Sequence similaritiesi

Belongs to the GMC oxidoreductase family.Curated

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR012132. GMC_OxRdtase.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamiPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000137. Alcohol_oxidase. 1 hit.
SUPFAMiSSF51905. SSF51905. 2 hits.
PROSITEiPS00623. GMC_OXRED_1. 1 hit.
PS00624. GMC_OXRED_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q00922-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIPEEFDVI VCGGGSTGCV IAGRLANVDE NLKVLLIENG ENNLNNPWVY
60 70 80 90 100
LPGIYPRNMR LDSKTATFYN SRPSKHLNGR RAIVPQANIL GGGSSINFMM
110 120 130 140 150
YTRASASDYD DWESEGWTTD ELLPLMKKFE TYQRPCNNRD VHGFDGPIKV
160 170 180 190 200
SFGNYTYPQC QDFLRACETQ GIPYVDDLED LKTSHGAEQW LKWINRDFGR
210 220 230 240 250
RSDTAHAFIH STMRNKENLF LMTNTKVDKV IIEDGRAVAV RTVPSKPIGD
260 270 280 290 300
SKVSRTFKAR KQIVVSCGTV SSPMVLQRSG IGEPSKLRAA GVKPIVELPG
310 320 330 340 350
VGRNFQDHFC YFVPYRIKQD SESFDAFVSG DKEAQKSAFD QWYATGAGPL
360 370 380 390 400
ATNGIEAGVK IRPTEAELAT ADKAFQQGWE SYFENKPDKP LMHYSVISGF
410 420 430 440 450
FGDHTRLPPG KYMTMFHFLE YPFSRGWLHI SSDDPYAAPD FDPGFMNDDR
460 470 480 490 500
DMWPMVWAFK KSRETARRME CFAGEPTAFH PHYKVDSPAR ALEQSAEDTK
510 520 530 540 550
KVAGPLHLTA NLYHGSWSTP IGEADKHDPN HVTSSHINVY SKDIQYTKED
560 570 580 590 600
DEAIENYIKE HAETTWHCLG TNSMAPREGN KNAPEGGVLD PRLNVHGVKG
610 620 630 640 650
LKVADLSVCP DNVGCNTFST ALTIGEKAAV LVAEDLGYSG SELDMEVPQH
660
KLKTYEQTGA ARY
Length:663
Mass (Da):74,082
Last modified:April 1, 1993 - v1
Checksum:iBC2E2F595B326AA6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81702 Genomic DNA. Translation: AAA34321.1.
PIRiJC1117.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81702 Genomic DNA. Translation: AAA34321.1.
PIRiJC1117.

3D structure databases

ProteinModelPortaliQ00922.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00147.
BioCyciMetaCyc:MONOMER-13165.
BRENDAi1.1.3.13. 1100.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR012132. GMC_OxRdtase.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamiPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000137. Alcohol_oxidase. 1 hit.
SUPFAMiSSF51905. SSF51905. 2 hits.
PROSITEiPS00623. GMC_OXRED_1. 1 hit.
PS00624. GMC_OXRED_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and sequencing of the alcohol oxidase-encoding gene (AOD1) from the formaldehyde-producing asporogeneous methylotrophic yeast, Candida boidinii S2."
    Sakai Y., Tani Y.
    Gene 114:67-73(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11; 13-18 AND 20-35, FUNCTION.
    Strain: S2.
  2. "Alcohol oxidase and dihydroxyacetone synthase, the abundant peroxisomal proteins of methylotrophic yeasts, assemble in different cellular compartments."
    Stewart M.Q., Esposito R.D., Gowani J., Goodman J.M.
    J. Cell Sci. 114:2863-2868(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, SUBUNIT.

Entry informationi

Entry nameiALOX_CANBO
AccessioniPrimary (citable) accession number: Q00922
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: November 11, 2015
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

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.