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Protein

Uncharacterized oxidoreductase At4g09670

Gene

At4g09670

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Enzyme and pathway databases

BioCyciARA:AT4G09670-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Uncharacterized oxidoreductase At4g09670 (EC:1.-.-.-)
Gene namesi
Ordered Locus Names:At4g09670
ORF Names:F17A8.20
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G09670.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 362361Uncharacterized oxidoreductase At4g09670PRO_0000091788Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9SZ83.
PRIDEiQ9SZ83.

PTM databases

iPTMnetiQ9SZ83.

Expressioni

Gene expression databases

GenevisibleiQ9SZ83. AT.

Interactioni

Subunit structurei

Homodimer.Curated

Protein-protein interaction databases

STRINGi3702.AT4G09670.1.

Structurei

Secondary structure

1
362
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 137Combined sources
Helixi18 – 2710Combined sources
Beta strandi31 – 377Combined sources
Helixi41 – 5010Combined sources
Beta strandi58 – 625Combined sources
Helixi63 – 686Combined sources
Beta strandi74 – 774Combined sources
Helixi81 – 833Combined sources
Helixi84 – 929Combined sources
Turni93 – 953Combined sources
Beta strandi97 – 1004Combined sources
Beta strandi105 – 1073Combined sources
Helixi108 – 11912Combined sources
Turni120 – 1223Combined sources
Beta strandi125 – 1273Combined sources
Helixi131 – 1333Combined sources
Helixi135 – 1373Combined sources
Turni138 – 1425Combined sources
Helixi143 – 1453Combined sources
Turni147 – 1504Combined sources
Beta strandi152 – 16312Combined sources
Helixi166 – 1716Combined sources
Helixi173 – 1753Combined sources
Helixi183 – 1875Combined sources
Helixi189 – 19911Combined sources
Turni200 – 2023Combined sources
Beta strandi206 – 2105Combined sources
Beta strandi222 – 2309Combined sources
Beta strandi232 – 2343Combined sources
Beta strandi236 – 26429Combined sources
Beta strandi273 – 2819Combined sources
Beta strandi288 – 2936Combined sources
Beta strandi296 – 3016Combined sources
Helixi306 – 3149Combined sources
Turni322 – 3243Combined sources
Helixi332 – 35120Combined sources
Turni352 – 3543Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YDWX-ray2.49A/B2-362[»]
2Q4EX-ray2.49A/B2-362[»]
ProteinModelPortaliQ9SZ83.
SMRiQ9SZ83. Positions 6-360.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9SZ83.

Family & Domainsi

Sequence similaritiesi

Belongs to the Gfo/Idh/MocA family.Curated

Phylogenomic databases

eggNOGiKOG2741. Eukaryota.
COG0673. LUCA.
HOGENOMiHOG000227440.
InParanoidiQ9SZ83.
OMAiHDFIIPY.
PhylomeDBiQ9SZ83.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR000683. Oxidoreductase_N.
[Graphical view]
PfamiPF01408. GFO_IDH_MocA. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9SZ83-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATETQIRIG VMGCADIARK VSRAIHLAPN ATISGVASRS LEKAKAFATA
60 70 80 90 100
NNYPESTKIH GSYESLLEDP EIDALYVPLP TSLHVEWAIK AAEKGKHILL
110 120 130 140 150
EKPVAMNVTE FDKIVDACEA NGVQIMDGTM WVHNPRTALL KEFLSDSERF
160 170 180 190 200
GQLKTVQSCF SFAGDEDFLK NDIRVKPGLD GLGALGDAGW YAIRATLLAN
210 220 230 240 250
NFELPKTVTA FPGAVLNEAG VILSCGASLS WEDGRTATIY CSFLANLTME
260 270 280 290 300
ITAIGTKGTL RVHDFIIPYK ETEASFTTST KAWFNDLVTA WVSPPSEHTV
310 320 330 340 350
KTELPQEACM VREFARLVGE IKNNGAKPDG YWPSISRKTQ LVVDAVKESV
360
DKNYQQISLS GR
Length:362
Mass (Da):39,562
Last modified:May 1, 2000 - v1
Checksum:iEC2595BE6C53AACC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti173 – 1731I → M in BAD94240 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL049482 Genomic DNA. Translation: CAB39634.1.
AL161515 Genomic DNA. Translation: CAB78090.1.
CP002687 Genomic DNA. Translation: AEE82779.1.
BT002355 mRNA. Translation: AAN86188.1.
AY045851 mRNA. Translation: AAK76525.2.
AY085911 mRNA. Translation: AAM63123.1.
AK220867 mRNA. Translation: BAD94240.1.
PIRiT04014.
RefSeqiNP_192705.1. NM_117035.3.
UniGeneiAt.23812.

Genome annotation databases

EnsemblPlantsiAT4G09670.1; AT4G09670.1; AT4G09670.
GeneIDi826553.
GrameneiAT4G09670.1; AT4G09670.1; AT4G09670.
KEGGiath:AT4G09670.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL049482 Genomic DNA. Translation: CAB39634.1.
AL161515 Genomic DNA. Translation: CAB78090.1.
CP002687 Genomic DNA. Translation: AEE82779.1.
BT002355 mRNA. Translation: AAN86188.1.
AY045851 mRNA. Translation: AAK76525.2.
AY085911 mRNA. Translation: AAM63123.1.
AK220867 mRNA. Translation: BAD94240.1.
PIRiT04014.
RefSeqiNP_192705.1. NM_117035.3.
UniGeneiAt.23812.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YDWX-ray2.49A/B2-362[»]
2Q4EX-ray2.49A/B2-362[»]
ProteinModelPortaliQ9SZ83.
SMRiQ9SZ83. Positions 6-360.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G09670.1.

PTM databases

iPTMnetiQ9SZ83.

Proteomic databases

PaxDbiQ9SZ83.
PRIDEiQ9SZ83.

Protocols and materials databases

DNASUi826553.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G09670.1; AT4G09670.1; AT4G09670.
GeneIDi826553.
GrameneiAT4G09670.1; AT4G09670.1; AT4G09670.
KEGGiath:AT4G09670.

Organism-specific databases

TAIRiAT4G09670.

Phylogenomic databases

eggNOGiKOG2741. Eukaryota.
COG0673. LUCA.
HOGENOMiHOG000227440.
InParanoidiQ9SZ83.
OMAiHDFIIPY.
PhylomeDBiQ9SZ83.

Enzyme and pathway databases

BioCyciARA:AT4G09670-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9SZ83.
PROiQ9SZ83.

Gene expression databases

GenevisibleiQ9SZ83. AT.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR000683. Oxidoreductase_N.
[Graphical view]
PfamiPF01408. GFO_IDH_MocA. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "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.
    , 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.
  4. "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].
  5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 173-362.
    Strain: cv. Columbia.
  6. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "X-ray structure of gene product from Arabidopsis thaliana At4g09670."
    Center for eukaryotic structural genomics (CESG)
    Submitted (JAN-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 2-362, SUBUNIT.

Entry informationi

Entry nameiY4967_ARATH
AccessioniPrimary (citable) accession number: Q9SZ83
Secondary accession number(s): Q56ZU4, Q94AR5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: May 1, 2000
Last modified: February 17, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  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.