Q52437 (Q52437_PSES1) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Ferredoxin reductase EMBL BAA04112.2

Gene names

Name:

bphA4 EMBL BAA04112.2

Organism

Pseudomonas sp. (strain KKS102) EMBL BAA04112.2

Taxonomic identifier

307 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria

Protein attributes

Sequence length	408 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	FAD PDB 1F3P PDB 2GQW PDB 2GR0 PDB 2GR1 PDB 2GR2 PDB 2GR3 PDB 2YVF PDB 2YVG PDB 1D7Y PDB 2YVJ Flavoprotein PDB 1F3P PDB 2GQW PDB 2GR0 PDB 2GR1 PDB 2GR2 PDB 2GR3 PDB 2YVF PDB 2YVG PDB 1D7Y PDB 2YVJ NAD PDB 1F3P PDB 2YVF PDB 2YVG PDB 2YVJ Nucleotide-binding PDB 1F3P PDB 2GQW PDB 2GR0 PDB 2GR1 PDB 2GR2 PDB 2GR3 PDB 2YVF PDB 2YVG PDB 1D7Y PDB 2YVJ
Technical term	3D-structure PDB 1F3P PDB 2GQW PDB 2GR0 PDB 2GR1 PDB 2GR2 PDB 2GR3 PDB 2YVF PDB 2YVG PDB 1D7Y PDB 2YVJ
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Nucleotide binding	17 – 18	2	FAD PDB 1F3P PDB 2GQW PDB 2GR0 PDB 2GR1 PDB 2GR2 PDB 2GR3 PDB 2YVF PDB 2YVG PDB 1D7Y PDB 2YVJ
	Nucleotide binding	40 – 41	2	FAD PDB 1F3P PDB 2GQW PDB 2GR0 PDB 2GR1 PDB 2GR2 PDB 2GR3 PDB 2YVF PDB 2YVG PDB 1D7Y PDB 2YVJ
	Nucleotide binding	48 – 49	2	FAD PDB 1F3P PDB 2GQW PDB 2GR0 PDB 2GR1 PDB 2GR2 PDB 2GR3 PDB 2YVF PDB 2YVG PDB 1D7Y PDB 2YVJ
	Nucleotide binding	152 – 159	8	NAD PDB 1F3P PDB 2YVF PDB 2YVG PDB 2YVJ
	Nucleotide binding	175 – 176	2	NAD PDB 1F3P PDB 2YVF PDB 2YVG PDB 2YVJ
	Nucleotide binding	182 – 183	2	NAD PDB 1F3P PDB 2YVF PDB 2YVG PDB 2YVJ
	Nucleotide binding	234 – 236	3	NAD PDB 1F3P PDB 2YVF PDB 2YVG PDB 2YVJ
	Nucleotide binding	289 – 291	3	FAD PDB 1F3P PDB 2GQW PDB 2GR0 PDB 2GR1 PDB 2GR2 PDB 2GR3 PDB 2YVF PDB 2YVG PDB 1D7Y PDB 2YVJ
	Nucleotide binding	319 – 320	2	NAD PDB 1F3P PDB 2YVF PDB 2YVG
Sites
	Binding site	53	1	FAD PDB 2GQW PDB 2GR0 PDB 2GR2 PDB 2GR3 PDB 1D7Y PDB 2YVJ
	Binding site	82	1	FAD; via amide nitrogen and carbonyl oxygen PDB 1F3P PDB 2GQW PDB 2GR0 PDB 2GR1 PDB 2GR2 PDB 2GR3 PDB 2YVF PDB 2YVG PDB 1D7Y PDB 2YVJ
	Binding site	109	1	FAD; via carbonyl oxygen PDB 2YVJ
	Binding site	114	1	NAD PDB 2YVF PDB 2YVG
	Binding site	130	1	FAD PDB 1F3P PDB 2GQW PDB 2GR0 PDB 2GR1 PDB 2GR2 PDB 2GR3 PDB 2YVF PDB 2YVG PDB 1D7Y PDB 2YVJ
	Binding site	130	1	NAD PDB 2YVF
	Binding site	159	1	FAD PDB 2GR1 PDB 2YVF
	Binding site	175	1	ADP PDB 2GR0
	Binding site	183	1	ADP PDB 2GR0
	Binding site	236	1	ADP; via amide nitrogen PDB 2GR0
	Binding site	273	1	FAD PDB 1F3P PDB 2GQW PDB 2GR0 PDB 2GR1 PDB 2GR2 PDB 2GR3 PDB 2YVF PDB 2YVG PDB 1D7Y PDB 2YVJ
	Binding site	273	1	NAD PDB 2YVF
	Binding site	289	1	NAD PDB 1F3P PDB 2YVF PDB 2YVG PDB 2YVJ
	Binding site	320	1	FAD PDB 1F3P PDB 2GQW PDB 2GR0 PDB 2GR1 PDB 2GR2 PDB 2YVF PDB 2YVG PDB 1D7Y PDB 2YVJ

Sequences

	Sequence		Length	Mass (Da)
	Q52437 [UniParc]. Last modified March 1, 2001. Version 2. Checksum: 253EB10E57E80844	FASTA	408	43,173
	10 20 30 40 50 60 MSQEALKAPV VVLGAGLASV SFVAELRQAG YQGLITVVGD EAERPYDRPP LSKDFMAHGD 70 80 90 100 110 120 AEKIRLDCKR APEVEWLLGV TAQSFDPQAH TVALSDGRTL PYGTLVLATG AAPRALPTLQ 130 140 150 160 170 180 GATMPVHTLR TLEDARRIQA GLRPQSRLLI VGGGVIGLEL AATARTAGVH VSLVETQPRL 190 200 210 220 230 240 MSRAAPATLA DFVARYHAAQ GVDLRFERSV TGSVDGVVLL DDGTRIAADM VVVGIGVLAN 250 260 270 280 290 300 DALARAAGLA CDDGIFVDAY GRTTCPDVYA LGDVTRQRNP LSGRFERIET WSNAQNQGIA 310 320 330 340 350 360 VARHLVDPTA PGYAELPWYW SDQGALRIQV AGLASGDEEI VRGEVSLDAP KFTLIELQKG 370 380 390 400 RIVGATCVNN ARDFAPLRRL LAVGAKPDRA ALADPATDLR KLAAAVAA

References

[1]	"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: 8132464] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: KKS102 EMBL BAA04112.2.
[2]	"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: KKS102 EMBL BAA04112.2.
[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: 11090282] [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 (1.80 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: 17850818] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH ADP; FAD AND NAD.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D16831 Genomic DNA. Translation: BAA04112.2.

PIR

B55523.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D7Y	X-ray	2.10	A	1-408	[»]
1F3P	X-ray	2.40	A	1-408	[»]
2GQW	X-ray	1.40	A	1-408	[»]
2GR0	X-ray	1.70	A	1-408	[»]
2GR1	X-ray	1.80	A	1-408	[»]
2GR2	X-ray	1.85	A	1-408	[»]
2GR3	X-ray	1.50	A	1-408	[»]
2YVF	X-ray	1.60	A	1-408	[»]
2YVG	X-ray	1.60	A	1-408	[»]
2YVJ	X-ray	1.90	A/P	1-408	[»]

ProteinModelPortal

Q52437.

SMR

Q52437. Positions 5-406.

ModBase

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Protocols and materials databases

StructuralBiologyKnowledgebase

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Family and domain databases

InterPro

IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR000103. Pyridine_nuc-diS_OxRdtase_2.
[Graphical view]

Gene3D

G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.

Pfam

PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]

PRINTS

PR00368. FADPNR.
PR00469. PNDRDTASEII.

SUPFAM

SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.

ProtoNet

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Entry information

Entry name

Q52437_PSES1

Accession

Primary (citable) accession number: Q52437

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1996
Last sequence update:	March 1, 2001
Last modified:	July 27, 2011
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)