Reviewed, UniProtKB/Swiss-Prot O67505 (FABI_AQUAE)

Names and origin

Protein names

Recommended name:
    Enoyl-[acyl-carrier-protein] reductase [NADH]
    EC=1.3.1.9
Alternative name(s):
    NADH-dependent enoyl-ACP reductase

Gene names

Name:	fabI
Ordered Locus Names:	aq_1552

Organism

Aquifex aeolicus [Complete proteome] [HAMAP]

Taxonomic identifier

63363 [NCBI]

Taxonomic lineage

Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length	270 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Acyl-[acyl-carrier-protein] + NAD+ = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADH.
Pathway	Lipid metabolism; fatty acid biosynthesis.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family. FabI subfamily.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	binding Inferred from electronic annotation. Source: InterPro enoyl-[acyl-carrier-protein] reductase (NADH) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 270

270

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

PRO_0000054894

Regions

Nucleotide binding

10 – 36

27

NAD By similarity

Sites

Active site

156

1

Proton acceptor By similarity

Secondary structure

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270

Helix Strand Turn

Details...

Turn

3 – 6

4

Beta strand

8 – 11

4

Helix

20 – 30

11

Beta strand

34 – 41

8

Helix

42 – 44

3

Helix

45 – 54

10

Beta strand

60 – 62

3

Helix

68 – 81

14

Beta strand

87 – 90

4

Helix

97 – 100

4

Helix

104 – 106

3

Helix

109 – 119

11

Helix

121 – 130

10

Helix

131 – 134

4

Beta strand

140 – 145

6

Helix

147 – 149

3

Turn

154 – 157

4

Helix

158 – 178

21

Turn

179 – 181

3

Beta strand

183 – 189

7

Helix

203 – 213

11

Helix

222 – 232

11

Helix

235 – 237

3

Beta strand

244 – 248

5

Helix

251 – 253

3

Sequences

	Sequence		Length	Mass (Da)
	O67505-1 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 2ACD6C85EE16DC68	FASTA	270	29,725
	10 20 30 40 50 60 MGLLEGKRAL ITGVANERSI AYGIAKSFHR EGAQLAFTYA TPKLEKRVRE IAKGFGSDLV 70 80 90 100 110 120 VKCDVSLDED IKNLKKFLEE NWGSLDIIVH SIAYAPKEEF KGGVIDTSRE GFKIAMDISV 130 140 150 160 170 180 YSLIALTREL LPLMEGRNGA IVTLSYYGAE KVVPHYNVMG IAKAALESTV RYLAYDIAKH 190 200 210 220 230 240 GHRINAISAG PVKTLAAYSI TGFHLLMEHT TKVNPFGKPI TIEDVGDTAV FLCSDWARAI 250 260 270 TGEVVHVDNG YHIMGVFGRE EEIKKEVYGD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus." Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V. Nature 392:353-358(1998) [PubMed: 9537320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VF5.
[2]	"Crystal structure of enoyl-[acyl-carrier-protein] reductase (NADH) from Aquifex aeolicus VF5." Southeast collaboratory for structural genomics (SECSG) Submitted (APR-2007) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

AE000657 Genomic DNA. Translation: AAC07465.1. Different initiation.

PIR

G70434.

RefSeq

NP_214070.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2P91	X-ray	2.00	A/B/C/D	1-270	[»]

ModBase

Search...

Genome annotation databases

GeneID

1193128.

GenomeReviews

Gene locus aq_1552 in contig AE000657_GR.

KEGG

aae:aq_1552.

NMPDR

fig|224324.1.peg.1085.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

O67505.

Enzyme and pathway databases

BioCyc

AAEO224324:AQ_1552-MON.

BRENDA

1.3.1.9. 189781.

Family and domain databases

InterPro

IPR002198. DH_sc/Rdtase_SDR.
IPR014358. Enoyl-ACP_Rdtase_NADH.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

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

PANTHER

PTHR19410. ADH_short_C2. 1 hit.
PTHR19410:SF12. Enoyl-ACP_rdct. 1 hit.

Pfam

PF00106. adh_short. 1 hit.
[Graphical view]

PRINTS

PR00081. GDHRDH.

ProtoNet

Search...

Entry information

Entry name

FABI_AQUAE

Accession

Primary (citable) accession number: O67505

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 30, 2000
Last modified:	June 16, 2009
This is version 62 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)