P54616 (FABI_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Enoyl-[acyl-carrier-protein] reductase [NADH] FabI
Short name=ENR
EC=1.3.1.9

Alternative name(s):
Cold shock-induced protein 15
Short name=CSI15
NADH-dependent enoyl-ACP reductase
Vegetative protein 241
Short name=VEG241

Gene names

Name:	fabI
Synonyms:	yjbW
Ordered Locus Names:	BSU11720

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	258 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism. Ref.4
Catalytic activity	Acyl-[acyl-carrier-protein] + NAD+ = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADH. Ref.4
Enzyme regulation	Inhibited by triclosan and acrylamide. Ref.4 Ref.5
Pathway	Lipid metabolism; fatty acid biosynthesis.
Subunit structure	Homotetramer. Ref.5
Induction	By cold shock. Ref.2 Ref.4 Ref.5
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family. FabI subfamily.
Biophysicochemical properties	Kinetic parameters: KM=7 µM for NADH Ref.4

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism Stress response
Ligand	NAD NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to cold Inferred from expression pattern Ref.2. Source: UniProtKB fatty acid elongation Inferred from direct assay Ref.4. Source: UniProtKB protein homotetramerization Inferred from direct assay Ref.5. Source: UniProtKB
Molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity Inferred from direct assay Ref.4. Source: UniProtKB 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

Chain

1 – 258

258

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

PRO_0000054895

Regions

Nucleotide binding

20 – 21

2

NAD

Nucleotide binding

67 – 68

2

NAD

Nucleotide binding

194 – 198

5

NAD

Sites

Active site

148

1

Proton acceptor By similarity

Active site

158

1

Proton acceptor

Binding site

14

1

NAD; via carbonyl oxygen

Binding site

95

1

NAD; via carbonyl oxygen

Binding site

98

1

Substrate; via amide nitrogen and carbonyl oxygen By similarity

Binding site

165

1

NAD

Site

206

1

Involved in acyl-ACP binding By similarity

Experimental info

Sequence conflict

20

1

S → Q AA sequence Ref.2

Secondary structure

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258

Helix Strand Turn

Details...

Beta strand

9 – 13

5

Helix

21 – 31

11

Beta strand

35 – 42

8

Helix

43 – 45

3

Helix

46 – 54

9

Beta strand

56 – 58

3

Beta strand

62 – 65

4

Beta strand

69 – 71

3

Helix

72 – 85

14

Beta strand

90 – 93

4

Helix

100 – 103

4

Helix

107 – 109

3

Helix

112 – 122

11

Helix

124 – 133

10

Helix

134 – 136

3

Beta strand

141 – 147

7

Helix

149 – 151

3

Turn

156 – 158

3

Helix

159 – 179

21

Helix

180 – 182

3

Beta strand

184 – 191

8

Helix

197 – 199

3

Beta strand

202 – 204

3

Helix

205 – 215

11

Helix

224 – 235

12

Helix

237 – 239

3

Beta strand

246 – 250

5

Helix

253 – 255

3

Sequences

	Sequence		Length	Mass (Da)
	P54616 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 097667168B3F0470	FASTA	258	27,874
	10 20 30 40 50 60 MNFSLEGRNI VVMGVANKRS IAWGIARSLH EAGARLIFTY AGERLEKSVH ELAGTLDRND 70 80 90 100 110 120 SIILPCDVTN DAEIETCFAS IKEQVGVIHG IAHCIAFANK EELVGEYLNT NRDGFLLAHN 130 140 150 160 170 180 ISSYSLTAVV KAARPMMTEG GSIVTLTYLG GELVMPNYNV MGVAKASLDA SVKYLAADLG 190 200 210 220 230 240 KENIRVNSIS AGPIRTLSAK GISDFNSILK DIEERAPLRR TTTPEEVGDT AAFLFSDMSR 250 GITGENLHVD SGFHITAR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[2]	"Cold shock stress-induced proteins in Bacillus subtilis." Graumann P., Schroeder K., Schmid R., Marahiel M.A. J. Bacteriol. 178:4611-4619(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-21, INDUCTION. Strain: 168 / JH642.
[3]	"First steps from a two-dimensional protein index towards a response-regulation map for Bacillus subtilis." Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M. Electrophoresis 18:1451-1463(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-15. Strain: 168 / IS58.
[4]	"The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis." Heath R.J., Su N., Murphy C.K., Rock C.O. J. Biol. Chem. 275:40128-40133(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS AN ENOYL-ACP REDUCTASE AND IN FATTY ACID BIOSYNTHESIS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[5]	"Crystal structures of Enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis." Kim K.H., Ha B.H., Kim S.J., Hong S.K., Hwang K.Y., Kim E.E. J. Mol. Biol. 406:403-415(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR, ENZYME REGULATION, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AL009126 Genomic DNA. Translation: CAB13029.2.

PIR

G69845.

RefSeq

NP_389054.2. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3OIF	X-ray	2.60	A/B/C/D	1-258	[»]
3OIG	X-ray	1.25	A	1-258	[»]

ProteinModelPortal

P54616.

SMR

P54616. Positions 1-258.

ModBase

Search...

Protein-protein interaction databases

STRING

224308.BSU11720.

Proteomic databases

PaxDb

P54616.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB13029; CAB13029; BSU11720.

GeneID

939379.

KEGG

bsu:BSU11720.

PATRIC

18974061. VBIBacSub10457_1224.

Organism-specific databases

GenoList

BSU11720. [Micado]

Phylogenomic databases

eggNOG

COG0623.

KO

K00208.

OMA

LVHCLAF.

ProtClustDB

PRK08594.

Enzyme and pathway databases

BioCyc

BSUB:BSU11720-MONOMER.

UniPathway

UPA00094.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.

InterPro

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

PIRSF

PIRSF000094. Enoyl-ACP_rdct. 1 hit.

PRINTS

PR00081. GDHRDH.

ProtoNet

Search...

Other

ChEMBL

CHEMBL1075044.

EvolutionaryTrace

P54616.

Entry information

Entry name

FABI_BACSU

Accession

Primary (citable) accession number: P54616
Secondary accession number(s): O31621

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	May 30, 2000
Last modified:	May 1, 2013
This is version 103 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program