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Q8GXX0 (ERV1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
FAD-linked sulfhydryl oxidase ERV1

Short name=AtErv1
EC=1.8.3.2
Alternative name(s):
Mitochondrial sulfhydryl oxidase ERV1
Gene names
Name:ERV1
Ordered Locus Names:At1g49880
ORF Names:F10F5.3
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length191 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation. Oxidizes thioredoxin in vitro. Ref.1

Catalytic activity

2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2.

Cofactor

FAD. Ref.1

Subunit structure

Homodimer. Ref.1 Ref.7

Subcellular location

Mitochondrion Ref.1.

Sequence similarities

Contains 1 ERV/ALR sulfhydryl oxidase domain.

Sequence caution

The sequence AAG51780.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 191191FAD-linked sulfhydryl oxidase ERV1
PRO_0000401377

Regions

Domain72 – 172101ERV/ALR sulfhydryl oxidase
Nucleotide binding81 – 844FAD
Nucleotide binding121 – 1255FAD
Nucleotide binding148 – 1558FAD
Nucleotide binding171 – 1722FAD
Motif177 – 1826Required for dimerization and substrate specificity

Sites

Binding site761FAD
Binding site1601FAD

Amino acid modifications

Disulfide bond119 ↔ 122Redox-active By similarity
Disulfide bond148 ↔ 165 Ref.7
Disulfide bond177 ↔ 182 Ref.7

Experimental info

Mutagenesis1771C → A: Loss the capacity to oxidize thioredoxin; when associated with A-182. Ref.7
Mutagenesis1821C → A: Loss the capacity to oxidize thioredoxin; when associated with A-177. Ref.7
Sequence conflict35 – 362PS → R in AAM63908. Ref.6

Secondary structure

........... 191
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8GXX0 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 7CC7FEA44C0D4B38

FASTA19121,600
        10         20         30         40         50         60 
MGEKPWQPLL QSFEKLSNCV QTHLSNFIGI KNTPPSSQST IQNPIISLDS SPPIATNSSS 

        70         80         90        100        110        120 
LQKLPLKDKS TGPVTKEDLG RATWTFLHTL AAQYPEKPTR QQKKDVKELM TILSRMYPCR 

       130        140        150        160        170        180 
ECADHFKEIL RSNPAQAGSQ EEFSQWLCHV HNTVNRSLGK LVFPCERVDA RWGKLECEQK 

       190 
SCDLHGTSMD F 

« Hide

References

« Hide 'large scale' references
[1]"Unique features of plant mitochondrial sulfhydryl oxidase."
Levitan A., Danon A., Lisowsky T.
J. Biol. Chem. 279:20002-20008(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION.
[2]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Functional annotation of a full-length Arabidopsis cDNA collection."
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K.
Science 296:141-145(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[6]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"Gain of function in an ERV/ALR sulfhydryl oxidase by molecular engineering of the shuttle disulfide."
Vitu E., Bentzur M., Lisowsky T., Kaiser C.A., Fass D.
J. Mol. Biol. 362:89-101(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 71-191 IN COMPLEX WITH FAD, SUBUNIT, DISULFIDE BONDS, MUTAGENESIS OF CYS-177 AND CYS-182.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ551263 mRNA. Translation: CAD83013.1.
AC079674 Genomic DNA. Translation: AAG51780.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE32487.1.
AK117991 mRNA. Translation: BAC42626.1.
BT003718 mRNA. Translation: AAO39946.1.
AY086861 mRNA. Translation: AAM63908.1.
PIRG96535.
RefSeqNP_564557.1. NM_103875.3.
UniGeneAt.38141.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HJ3X-ray2.50A/B71-191[»]
ProteinModelPortalQ8GXX0.
SMRQ8GXX0. Positions 73-173.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT1G49880.1-P.

Proteomic databases

PaxDbQ8GXX0.
PRIDEQ8GXX0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G49880.1; AT1G49880.1; AT1G49880.
GeneID841411.
KEGGath:AT1G49880.

Organism-specific databases

TAIRAT1G49880.

Phylogenomic databases

eggNOGCOG5054.
HOGENOMHOG000120834.
InParanoidQ8GXX0.
KOK17783.
OMAIFPCQRV.
PhylomeDBQ8GXX0.

Enzyme and pathway databases

BioCycARA:AT1G49880-MONOMER.

Gene expression databases

GenevestigatorQ8GXX0.

Family and domain databases

Gene3D1.20.120.310. 1 hit.
InterProIPR017905. ERV/ALR_sulphydryl_oxidase.
[Graphical view]
PfamPF04777. Evr1_Alr. 1 hit.
[Graphical view]
SUPFAMSSF69000. SSF69000. 1 hit.
PROSITEPS51324. ERV_ALR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8GXX0.
PROQ8GXX0.

Entry information

Entry nameERV1_ARATH
AccessionPrimary (citable) accession number: Q8GXX0
Secondary accession number(s): Q8LC15, Q9C6C6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: March 1, 2003
Last modified: May 14, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names