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Protein
Submitted name:

FAD-dependent oxidoreductase

Gene

KijD3

Organism
Actinomadura kijaniata
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei171 – 1711FMNCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi141 – 1433FMNCombined sources
Nucleotide bindingi383 – 3853FMNCombined sources

GO - Molecular functioni

  1. acyl-CoA dehydrogenase activity Source: InterPro
  2. flavin adenine dinucleotide binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotation

Keywords - Ligandi

FADUniRule annotation, Flavoprotein, FMNCombined sources, Nucleotide-bindingCombined sources

Names & Taxonomyi

Protein namesi
Submitted name:
FAD-dependent oxidoreductaseImported
Gene namesi
ORF Names:KijD3Imported
OrganismiActinomadura kijaniataImported
Taxonomic identifieri46161 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptosporangineaeThermomonosporaceaeActinomadura

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3M9VX-ray2.05A1-437[»]
4KCFX-ray2.10A1-437[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.UniRule annotation

Family and domain databases

Gene3Di1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProiIPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view]
PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.

Sequencei

Sequence statusi: Complete.

B3TMR1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPPWTARQDS TTGLYAPVTP AGRVLLDRLA AHLPRIRSTA AEHDRDGTFP
60 70 80 90 100
TDTFDALRKD GLMGATVPAE LGGLGVDRLY DVAVALLAVA RADASTALAL
110 120 130 140 150
HMQLSRGLTL GYEWRHGDER ARTLAERILR GMVAGDAVVC SGIKDHHTAV
160 170 180 190 200
TTLRPDGAGG WLLSGRKTLV SMAPVGTHFV INARTDGTDG PPRLASPVVT
210 220 230 240 250
RDTPGFTVLD NWDGLGMRAS GTVDIVFDDC PIPADHVLMR DPVGARNDAV
260 270 280 290 300
LAGQTVSSVS VLGVYVGVAQ AAYDTAVAAL ERRPEPPQAA ALTLVAEIDS
310 320 330 340 350
RLYALRATAG SALTAADALS ADLSGDMDER GRQMMRHFQC AKLAVNRLAP
360 370 380 390 400
EIVSDCLSLV GGASYTAGHP LARLLRDVQA GRFMQPYAYV DAVDFLSAQA
410 420 430
LGIERDNNYM STWAKRSGGN GKSADAAGPR RPTPTSR
Length:437
Mass (Da):46,240
Last modified:September 2, 2008 - v1
Checksum:i5ACFDC5E754820DB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU301739 Genomic DNA. Translation: ACB46491.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU301739 Genomic DNA. Translation: ACB46491.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3M9VX-ray2.05A1-437[»]
4KCFX-ray2.10A1-437[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProiIPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view]
PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Elucidation of the kijanimicin gene cluster: insights into the biosynthesis of spirotetronate antibiotics and nitrosugars."
    Zhang H., White-Phillip J.A., Melancon C.E., Kwon H.-J., Yu W.-L., Liu H.-W.
    J. Am. Chem. Soc. 129:14670-14683(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "X-ray structure of kijd3, a key enzyme involved in the biosynthesis of D-kijanose."
    Bruender N.A., Thoden J.B., Holden H.M.
    Biochemistry 49:3517-3524(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
  3. "Active site architecture of a sugar N-oxygenase."
    Thoden J.B., Branch M.C., Zimmer A.L., Bruender N.A., Holden H.M.
    Biochemistry 52:3191-3193(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH FMN.

Entry informationi

Entry nameiB3TMR1_9ACTO
AccessioniPrimary (citable) accession number: B3TMR1
Entry historyi
Integrated into UniProtKB/TrEMBL: September 2, 2008
Last sequence update: September 2, 2008
Last modified: January 7, 2015
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

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 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.