Reviewed, UniProtKB/Swiss-Prot Q39172 (P1_ARATH)

Names and origin

Protein names

Recommended name:
    Probable NADP-dependent oxidoreductase P1
    EC=1.3.1.74

Gene names

Name:	P1
Ordered Locus Names:	At5g16970
ORF Names:	F2K13_120

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	345 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May play a distinct role in plant antioxidant defense and is possibly involved in NAD(P)/NAD(P)h homeostasis.
Catalytic activity	n-alkanal + NAD(P)+ = alk-2-enal + NAD(P)H.
Sequence similarities	Belongs to the NADP-dependent oxidoreductase L4BD family.

Ontologies

Keywords
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to cadmium ion Inferred from expression pattern. Source: TAIR response to oxidative stress Ref.1 Inferred from mutant phenotype. Source: TAIR
Cellular component	cytosol Inferred from direct assay. Source: TAIR nucleus Inferred from direct assay. Source: TAIR
Molecular function	2-alkenal reductase activity Inferred from direct assay. Source: TAIR zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 345

345

Probable NADP-dependent oxidoreductase P1

PRO_0000218073

Secondary structure

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345

Helix Strand Turn

Details...

Beta strand

2 – 10

9

Beta strand

14 – 17

4

Helix

20 – 22

3

Beta strand

23 – 31

9

Beta strand

36 – 39

4

Beta strand

41 – 45

5

Beta strand

47 – 49

3

Helix

54 – 58

5

Beta strand

79 – 89

11

Beta strand

99 – 112

14

Turn

116 – 118

3

Beta strand

120 – 122

3

Helix

131 – 133

3

Turn

134 – 136

3

Helix

138 – 148

11

Beta strand

158 – 163

6

Helix

167 – 178

12

Beta strand

182 – 189

8

Helix

190 – 198

9

Beta strand

203 – 207

5

Helix

215 – 221

7

Beta strand

226 – 233

8

Helix

235 – 242

8

Beta strand

245 – 253

9

Helix

257 – 259

3

Helix

273 – 277

5

Beta strand

280 – 283

4

Helix

286 – 292

7

Helix

293 – 305

13

Beta strand

313 – 318

6

Helix

319 – 321

3

Helix

323 – 330

8

Beta strand

335 – 343

9

Sequences

	Sequence		Length	Mass (Da)
	Q39172-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 5AFCEBB2948B2680	FASTA	345	38,134
	10 20 30 40 50 60 MTATNKQVIL KDYVSGFPTE SDFDFTTTTV ELRVPEGTNS VLVKNLYLSC DPYMRIRMGK 70 80 90 100 110 120 PDPSTAALAQ AYTPGQPIQG YGVSRIIESG HPDYKKGDLL WGIVAWEEYS VITPMTHAHF 130 140 150 160 170 180 KIQHTDVPLS YYTGLLGMPG MTAYAGFYEV CSPKEGETVY VSAASGAVGQ LVGQLAKMMG 190 200 210 220 230 240 CYVVGSAGSK EKVDLLKTKF GFDDAFNYKE ESDLTAALKR CFPNGIDIYF ENVGGKMLDA 250 260 270 280 290 300 VLVNMNMHGR IAVCGMISQY NLENQEGVHN LSNIIYKRIR IQGFVVSDFY DKYSKFLEFV 310 320 330 340 LPHIREGKIT YVEDVADGLE KAPEALVGLF HGKNVGKQVV VVARE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Arabidopsis thaliana NADPH oxidoreductase homologs confer tolerance of yeasts toward the thiol-oxidizing drug diamide." Babiychuk E., Kushnir S., Belles-Boix E., van Montagu M., Inze D. J. Biol. Chem. 270:26224-26231(1995) [PubMed: 7592828] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F. Nature 408:823-826(2000) [PubMed: 11130714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z49768 mRNA. Translation: CAA89838.1.
AL391141 Genomic DNA. Translation: CAC01710.1.

IPI

IPI00542017.

PIR

S57611.

RefSeq

NP_197199.1.

UniGene

At.22432

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2J3H	X-ray	2.50	A/B	1-345	[»]
2J3I	X-ray	2.80	A/B	1-345	[»]
2J3J	X-ray	2.80	A/B	1-345	[»]
2J3K	X-ray	2.80	A/B	1-345	[»]

ModBase

Search...

Proteomic databases

PRIDE

Q39172.

ProMEX

Q39172.

Genome annotation databases

GeneID

831560.

GenomeReviews

Gene locus AT5G16970 in contig BA000015_GR.

KEGG

ath:AT5G16970.

Organism-specific databases

TAIR

At5g16970.

Phylogenomic databases

eggNOG

KOG1196.

HOGENOM

HBG753318.

InParanoid

Q39172.

OMA

RIRPLEN.

PhylomeDB

Q39172.

Enzyme and pathway databases

BRENDA

1.3.1.74. 302.

Gene expression databases

Genevestigator

Q39172.

GermOnline

AT5G16970. Arabidopsis thaliana.

Family and domain databases

InterPro

IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

PANTHER

PTHR11695. ADH_Sf_Zn. 1 hit.

Pfam

PF00107. ADH_zinc_N. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

P1_ARATH

Accession

Primary (citable) accession number: Q39172

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	February 9, 2010
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)