[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-27, AND CHARACTERIZATION. PubMed=9922271 [NCBI, ExPASy, EBI, Israel, Japan] Boonstra B., French C.E., Wainwright I., Bruce N.C.; "The udhA gene of Escherichia coli encodes a soluble pyridine nucleotide transhydrogenase."; J. Bacteriol. 181:1030-1034(1999).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1093/nar/21.23.5408; PubMed=8265357 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.; "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."; Nucleic Acids Res. 21:5408-5417(1993).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-346. STRAIN=K12; PubMed=1447162 [NCBI, ExPASy, EBI, Israel, Japan] Gustafsson C., Warne S.R.; "Physical map of the oxyR-trmA region (minute 89.3) of the Escherichia coli chromosome."; J. Bacteriol. 174:7878-7879(1992).
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 347-466. DOI=10.1007/BF00332397; PubMed=2511419 [NCBI, ExPASy, EBI, Israel, Japan] Tao K., Makino K., Yonei S., Nakata A., Shinagawa H.; "Molecular cloning and nucleotide sequencing of oxyR, the positive regulatory gene of a regulon for an adaptive response to oxidative stress in Escherichia coli: homologies between OxyR protein and a family of bacterial activator proteins."; Mol. Gen. Genet. 218:371-376(1989).

Comments

FUNCTION: Conversion of NADPH, generated by peripheral catabolic pathways, to NADH, which can enter the respiratory chain for energy generation.
CATALYTIC ACTIVITY: NADPH + NAD⁺ = NADP⁺ + NADH.
COFACTOR: Binds 1 FAD per subunit.
SUBUNIT: Homooligomer; probable homooctamer.
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
SEQUENCE CAUTION:
- Sequence=AAC43068.1; Type=Frameshift; Positions=15;
- Sequence=CAA46822.1; Type=Frameshift; Positions=15;

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U00006; AAC43068.1; ALT_FRAME; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76944.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77349.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X66026; CAA46822.1; ALT_FRAME; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X16531; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]

PIR

E65203; E65203.

RefSeq

AP_003848.1; -.
NP_418397.2; -.

3D structure databases

HSSP

P14218; 1LPF. [HSSP ENTRY / PDB]

ModBase

P27306.

Protein-protein interaction databases

IntAct

P27306; -.

Enzyme and pathway databases

BioCyc

EcoCyc:UDHA-MON; -.
MetaCyc:UDHA-MON; -.

Organism-specific databases

EchoBASE

EB1398; -.

EcoGene

EG11428; sthA.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0003957;	Molecular function: NAD(P)+ transhydrogenase (B-specific) activity (inferred from electronic annotation from HAMAP).
GO:0006739;	Biological process: NADP metabolic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00247; -; 1.
PBIL [Tree]

InterPro

IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR000815; Hg_reductase.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
IPR001327; Pyr_OxRdtase_NAD_bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.390.30; Pyr_redox_dim; 1.

Pfam

PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
PF02852; Pyr_redox_dim; 1.
Pfam graphical view of domain structure.

PRINTS

PR00368; FADPNR.
PR00945; HGRDTASE.
PR00411; PNDRDTASEI.

ProDom

PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]

BLOCKS

P27306.

Genome annotation databases

GeneID

948461; -.

GenomeReviews

U00096_GR; b3962.
AP009048_GR; JW5551.

KEGG

ecj:JW5551; -.
eco:b3962; -.

Phylogenomic databases

HOGENOM

P27306; -.

Genome annotation databases

CMR

P27306; b3962.

Other

ProtoNet

P27306.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; NAD; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 466`	`465`	`Soluble pyridine nucleotide transhydrogenase.`	`PRO_0000068061`
`NP_BIND`	`36 45`	`10`	`FAD (By similarity).`
`CONFLICT`	`64 64`		`I -> L (in Ref. 5; CAA46822).`
`CONFLICT`	`118 118`		`R -> L (in Ref. 5; CAA46822).`

Sequence information

Length: 466 AA [This is the length of the unprocessed precursor]

Molecular weight: 51560 Da [This is the MW of the unprocessed precursor]

CRC64: 2D7405D1E2D062FD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPHSYDYDAI VIGSGPGGEG AAMGLVKQGA RVAVIERYQN VGGGCTHWGT IPSKALRHAV 

        70         80         90        100        110        120 
SRIIEFNQNP LYSDHSRLLR SSFADILNHA DNVINQQTRM RQGFYERNHC EILQGNARFV 

       130        140        150        160        170        180 
DEHTLALDCP DGSVETLTAE KFVIACGSRP YHPTDVDFTH PRIYDSDSIL SMHHEPRHVL 

       190        200        210        220        230        240 
IYGAGVIGCE YASIFRGMDV KVDLINTRDR LLAFLDQEMS DSLSYHFWNS GVVIRHNEEY 

       250        260        270        280        290        300 
EKIEGCDDGV IMHLKSGKKL KADCLLYANG RTGNTDSLAL QNIGLETDSR GQLKVNSMYQ 

       310        320        330        340        350        360 
TAQPHVYAVG DVIGYPSLAS AAYDQGRIAA QALVKGEATA HLIEDIPTGI YTIPEISSVG 

       370        380        390        400        410        420 
KTEQQLTAMK VPYEVGRAQF KHLARAQIVG MNVGTLKILF HRETKEILGI HCFGERAAEI 

       430        440        450        460 
IHIGQAIMEQ KGGGNTIEYF VNTTFNYPTM AEAYRVAALN GLNRLF

P27306 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools