P80030 (FABI_BRANA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Enoyl-[acyl-carrier-protein] reductase [NADH], chloroplastic EC=1.3.1.9 Alternative name(s): NADH-dependent enoyl-ACP reductase
Organism	Brassica napus (Rape)
Taxonomic identifier	3708 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Brassiceae › Brassica

Protein attributes

Sequence length	385 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the NAD-dependent reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Catalyzes the last reduction step in the de novo synthesis cycle of fatty acids. Involved in the elongation cycle of fatty acids which are used in lipid metabolism. Required for normal plant growth By similarity.
Catalytic activity	Acyl-[acyl-carrier-protein] + NAD+ = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADH.
Enzyme regulation	Inactivated by phenylglyoxal by binding covalently to two arginine residues.
Pathway	Lipid metabolism; fatty acid biosynthesis.
Subunit structure	Homotetramer. Ref.3
Subcellular location	Plastid › chloroplast Potential.
Tissue specificity	Seeds and leaves.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family. FabI subfamily.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity Inferred from electronic annotation. Source: EC nucleotide 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

Transit peptide

1 – 73

73

Chloroplast Ref.1 Ref.2

Chain

74 – 385

312

Enoyl-[acyl-carrier-protein] reductase [NADH], chloroplastic

PRO_0000031984

Regions

Nucleotide binding

162 – 163

2

NAD

Nucleotide binding

209 – 210

2

NAD

Nucleotide binding

309 – 313

5

NAD

Sites

Active site

261

1

Proton acceptor By similarity

Active site

271

1

Proton acceptor By similarity

Binding site

98

1

NAD; via carbonyl oxygen

Binding site

105

1

NAD

Binding site

259

1

NAD; via carbonyl oxygen

Binding site

279

1

NAD

Natural variations

Natural variant

333

1

I → V.

Experimental info

Sequence conflict

104

1

G → A AA sequence Ref.2

Sequence conflict

109

1

V → I AA sequence Ref.2

Sequence conflict

280 – 281

2

AA → N AA sequence Ref.2

Secondary structure

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385

Helix Strand Turn

Details...

Beta strand

93 – 97

5

Beta strand

100 – 104

5

Helix

105 – 115

11

Beta strand

119 – 125

7

Helix

126 – 137

12

Turn

138 – 142

5

Helix

143 – 145

3

Beta strand

150 – 152

3

Beta strand

155 – 161

7

Helix

168 – 170

3

Helix

173 – 176

4

Helix

179 – 183

5

Helix

189 – 200

12

Beta strand

203 – 208

6

Turn

214 – 217

4

Helix

220 – 222

3

Helix

225 – 235

11

Helix

237 – 246

10

Helix

247 – 249

3

Beta strand

250 – 260

11

Helix

262 – 264

3

Turn

272 – 274

3

Helix

275 – 297

23

Beta strand

300 – 306

7

Helix

312 – 317

6

Helix

319 – 330

12

Beta strand

331 – 333

3

Helix

339 – 349

11

Helix

352 – 354

3

Beta strand

361 – 365

5

Helix

368 – 370

3

Helix

378 – 380

3

Sequences

	Sequence		Length	Mass (Da)
	P80030 [UniParc]. Last modified February 1, 1994. Version 2. Checksum: C435BCE32A8D059B	FASTA	385	40,479
	10 20 30 40 50 60 MAATAAASSL QMATTRPSIS AASSKARTYV VGANPRNAYK IACTPHLSNL GCLRNDSALP 70 80 90 100 110 120 ASKKSFSFST KAMSESSESK ASSGLPIDLR GKRAFIAGIA DDNGYGWAVA KSLAAAGAEI 130 140 150 160 170 180 LVGTWVPALN IFETSLRRGK FDQSRVLPDG SLMEIKKVYP LDAVFDNPED VPEDVKANKR 190 200 210 220 230 240 YAGSSNWTVQ EAAECVRQDF GSIDILVHSL ANGPEVSKPL LETSRKGYLA AISASSYSFV 250 260 270 280 290 300 SLLSHFLPIM NPGGASISLT YIASERIIPG YGGGMSSAKA ALESDTRVLA FEAGRKQNIR 310 320 330 340 350 360 VNTISAGPLG SRAAKAIGFI DTMIEYSYNN APIQKTLTAD EVGNAAAFLV SPLASAITGA 370 380 TIYVDNGLNS MGVALDSPVF KDLNK

References

[1]	"cDNA cloning and expression of Brassica napus enoyl-acyl carrier protein reductase in Escherichia coli." Kater M.M., Koningstein G.M., Nijkamp H.J., Stuitje A.R. Plant Mol. Biol. 17:895-909(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 74-86. Strain: cv. Rafal.
[2]	"Amino acid sequence analysis of rape seed (Brassica napus) NADH-enoyl ACP reductase." Slabas A.R., Cottingham I., Austin A., Fawcett T., Sidebottom C.M. Plant Mol. Biol. 17:911-914(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 74-122; 146-174; 181-193; 250-295; 301-311; 316-346 AND 371-385. Tissue: Seed.
[3]	"Common themes in redox chemistry emerge from the X-ray structure of oilseed rape (Brassica napus) enoyl acyl carrier protein reductase." Rafferty J.B., Simon J.W., Baldock C., Artymiuk P.J., Baker P.J., Stuitje A.R., Slabas A.R., Rice D.W. Structure 3:927-938(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 74-383 IN COMPLEX WITH NAD, SUBUNIT.
[4]	"Inhibitor binding studies on enoyl reductase reveal conformational changes related to substrate recognition." Roujeinikova A., Sedelnikova S., de Boer G.J., Stuitje A.R., Slabas A.R., Rafferty J.B., Rice D.W. J. Biol. Chem. 274:30811-30817(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 85-380 IN COMPLEX WITH NAD.
[5]	"Crystallographic analysis of triclosan bound to enoyl reductase." Roujeinikova A., Levy C.W., Rowsell S., Sedelnikova S., Baker P.J., Minshull C.A., Mistry A., Colls J.G., Camble R., Stuitje A.R., Slabas A.R., Rafferty J.B., Pauptit R.A., Viner R., Rice D.W. J. Mol. Biol. 294:527-535(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 84-380 IN COMPLEX WITH NAD.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

S60064 mRNA. Translation: AAB20114.2.

PIR

S17761.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CWU	X-ray	2.50	A/B	85-380	[»]
1D7O	X-ray	1.90	A	84-380	[»]
1ENO	X-ray	1.90	A	74-383	[»]
1ENP	X-ray	2.60	A	74-383	[»]

ProteinModelPortal

P80030.

SMR

P80030. Positions 84-380.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

UniPathway

UPA00094.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.

InterPro

IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

PRINTS

PR00081. GDHRDH.

PROSITE

PS00061. ADH_SHORT. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P80030.

Entry information

Entry name

FABI_BRANA

Accession

Primary (citable) accession number: P80030

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	February 1, 1994
Last modified:	April 3, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program