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Protein
Submitted name:

Ferredoxin reductase

Gene

bphA4

Organism
Pseudomonas sp. (strain KKS102)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531FADCombined sources
Binding sitei82 – 821FAD; via amide nitrogen and carbonyl oxygenCombined sources
Binding sitei109 – 1091FAD; via carbonyl oxygenCombined sources
Binding sitei114 – 1141NADCombined sources
Binding sitei130 – 1301FADCombined sources
Binding sitei130 – 1301NADCombined sources
Binding sitei159 – 1591FADCombined sources
Binding sitei175 – 1751ADPCombined sources
Binding sitei183 – 1831ADPCombined sources
Binding sitei236 – 2361ADP; via amide nitrogenCombined sources
Binding sitei273 – 2731FADCombined sources
Binding sitei273 – 2731NADCombined sources
Binding sitei289 – 2891NADCombined sources
Binding sitei320 – 3201FADCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi17 – 182FADCombined sources
Nucleotide bindingi40 – 412FADCombined sources
Nucleotide bindingi48 – 492FADCombined sources
Nucleotide bindingi152 – 1598NADCombined sources
Nucleotide bindingi175 – 1762NADCombined sources
Nucleotide bindingi182 – 1832NADCombined sources
Nucleotide bindingi234 – 2363NADCombined sources
Nucleotide bindingi289 – 2913FADCombined sources
Nucleotide bindingi319 – 3202NADCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

FADCombined sources, Flavoprotein, NADCombined sources, Nucleotide-bindingCombined sources

Names & Taxonomyi

Protein namesi
Submitted name:
Ferredoxin reductaseImported
Gene namesi
Name:bphA4Imported
OrganismiPseudomonas sp. (strain KKS102)Imported
Taxonomic identifieri307 [NCBI]
Taxonomic lineageiBacteriaProteobacteria

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D7YX-ray2.10A1-408[»]
1F3PX-ray2.40A1-408[»]
2GQWX-ray1.40A1-408[»]
2GR0X-ray1.70A1-408[»]
2GR1X-ray1.80A1-408[»]
2GR2X-ray1.85A1-408[»]
2GR3X-ray1.50A1-408[»]
2YVFX-ray1.60A1-408[»]
2YVGX-ray1.60A1-408[»]
2YVJX-ray1.90A/P1-408[»]
ProteinModelPortaliQ52437.
SMRiQ52437. Positions 5-406.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ52437.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 298289FAD/NAD-binding_domInterPro annotationAdd
BLAST
Domaini318 – 40386Reductase_CInterPro annotationAdd
BLAST

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR028202. Reductase_C.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF14759. Reductase_C. 1 hit.
[Graphical view]
PRINTSiPR00469. PNDRDTASEII.
SUPFAMiSSF51905. SSF51905. 2 hits.
SSF55424. SSF55424. 1 hit.

Sequencei

Sequence statusi: Complete.

Q52437-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQEALKAPV VVLGAGLASV SFVAELRQAG YQGLITVVGD EAERPYDRPP
60 70 80 90 100
LSKDFMAHGD AEKIRLDCKR APEVEWLLGV TAQSFDPQAH TVALSDGRTL
110 120 130 140 150
PYGTLVLATG AAPRALPTLQ GATMPVHTLR TLEDARRIQA GLRPQSRLLI
160 170 180 190 200
VGGGVIGLEL AATARTAGVH VSLVETQPRL MSRAAPATLA DFVARYHAAQ
210 220 230 240 250
GVDLRFERSV TGSVDGVVLL DDGTRIAADM VVVGIGVLAN DALARAAGLA
260 270 280 290 300
CDDGIFVDAY GRTTCPDVYA LGDVTRQRNP LSGRFERIET WSNAQNQGIA
310 320 330 340 350
VARHLVDPTA PGYAELPWYW SDQGALRIQV AGLASGDEEI VRGEVSLDAP
360 370 380 390 400
KFTLIELQKG RIVGATCVNN ARDFAPLRRL LAVGAKPDRA ALADPATDLR

KLAAAVAA
Length:408
Mass (Da):43,173
Last modified:March 1, 2001 - v2
Checksum:i253EB10E57E80844
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16831 Genomic DNA. Translation: BAA04112.2.
PIRiB55523.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16831 Genomic DNA. Translation: BAA04112.2.
PIRiB55523.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D7YX-ray2.10A1-408[»]
1F3PX-ray2.40A1-408[»]
2GQWX-ray1.40A1-408[»]
2GR0X-ray1.70A1-408[»]
2GR1X-ray1.80A1-408[»]
2GR2X-ray1.85A1-408[»]
2GR3X-ray1.50A1-408[»]
2YVFX-ray1.60A1-408[»]
2YVGX-ray1.60A1-408[»]
2YVJX-ray1.90A/P1-408[»]
ProteinModelPortaliQ52437.
SMRiQ52437. Positions 5-406.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ52437.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
IPR028202. Reductase_C.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF14759. Reductase_C. 1 hit.
[Graphical view]
PRINTSiPR00469. PNDRDTASEII.
SUPFAMiSSF51905. SSF51905. 2 hits.
SSF55424. SSF55424. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Crystal structure of NADH-dependent ferredoxin reductase component in biphenyl dioxygenase."
    Senda T., Yamada T., Sakurai N., Kubota M., Nishizaki T., Masai E., Fukuda M., Mitsui Y.
    Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: KKS102Imported.
  2. "Identification of the bphA4 gene encoding ferredoxin reductase involved in biphenyl and polychlorinated biphenyl degradation in Pseudomonas sp. strain KKS102."
    Kikuchi Y., Nagata Y., Hinata M., Kimbara K., Fukuda M., Yano K., Takagi M.
    J. Bacteriol. 176:1689-1694(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: KKS102Imported.
  3. "Crystal structure of NADH-dependent ferredoxin reductase component in biphenyl dioxygenase."
    Senda T., Yamada T., Sakurai N., Kubota M., Nishizaki T., Masai E., Fukuda M., Mitsuidagger Y.
    J. Mol. Biol. 304:397-410(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH FAD AND NAD.
  4. "A ferredoxin reductase BphA4 uses a butterfly motion of FAD to regulate affinity for ferredoxin."
    Senda M., Kishigami S., Kimura S., Ishida T., Fukuda M., Senda T.
    Submitted (APR-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH FAD, X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH FAD, X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH FAD.
  5. "Molecular mechanism of the redox-dependent interaction between NADH-dependent ferredoxin reductase and Rieske-type [2Fe-2S] ferredoxin."
    Senda M., Kishigami S., Kimura S., Fukuda M., Ishida T., Senda T.
    J. Mol. Biol. 373:382-400(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH ADP; FAD AND NAD.

Entry informationi

Entry nameiQ52437_PSES1
AccessioniPrimary (citable) accession number: Q52437
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: March 1, 2001
Last modified: April 13, 2016
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.