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P54616

- FABI_BACSU

UniProt

P54616 - FABI_BACSU

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Protein

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

Gene

fabI

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

An acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH.1 Publication

Enzyme regulationi

Inhibited by triclosan and acrylamide.2 Publications

Kineticsi

  1. KM=7 µM for NADH1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei14 – 141NAD; via carbonyl oxygen1 Publication
Binding sitei95 – 951NAD; via carbonyl oxygen1 Publication
Binding sitei98 – 981Substrate; via amide nitrogen and carbonyl oxygenBy similarity
Active sitei148 – 1481Proton acceptorBy similarity
Active sitei158 – 1581Proton acceptor
Binding sitei165 – 1651NAD1 Publication
Sitei206 – 2061Involved in acyl-ACP bindingBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi20 – 212NAD1 Publication
Nucleotide bindingi67 – 682NAD1 Publication
Nucleotide bindingi194 – 1985NAD1 Publication

GO - Molecular functioni

  1. enoyl-[acyl-carrier-protein] reductase (NADH) activity Source: UniProtKB

GO - Biological processi

  1. cellular response to cold Source: UniProtKB
  2. fatty acid elongation Source: UniProtKB
  3. protein homotetramerization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Stress response

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

BioCyciBSUB:BSU11720-MONOMER.
SABIO-RKP54616.
UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
Enoyl-[acyl-carrier-protein] reductase [NADH] FabI (EC:1.3.1.9)
Short name:
ENR
Alternative name(s):
Cold shock-induced protein 15
Short name:
CSI15
NADH-dependent enoyl-ACP reductase
Vegetative protein 241
Short name:
VEG241
Gene namesi
Name:fabI
Synonyms:yjbW
Ordered Locus Names:BSU11720
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU11720. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 258258Enoyl-[acyl-carrier-protein] reductase [NADH] FabIPRO_0000054895Add
BLAST

Proteomic databases

PaxDbiP54616.

Expressioni

Inductioni

By cold shock.1 Publication

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

IntActiP54616. 1 interaction.
MINTiMINT-8366040.
STRINGi224308.BSU11720.

Structurei

Secondary structure

1
258
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 135Combined sources
Helixi21 – 3111Combined sources
Beta strandi35 – 428Combined sources
Helixi43 – 453Combined sources
Helixi46 – 549Combined sources
Beta strandi56 – 583Combined sources
Beta strandi62 – 654Combined sources
Beta strandi69 – 713Combined sources
Helixi72 – 8514Combined sources
Beta strandi90 – 934Combined sources
Helixi100 – 1034Combined sources
Helixi107 – 1093Combined sources
Helixi112 – 12211Combined sources
Helixi124 – 13310Combined sources
Helixi134 – 1363Combined sources
Beta strandi141 – 1477Combined sources
Helixi149 – 1513Combined sources
Turni156 – 1583Combined sources
Helixi159 – 17921Combined sources
Helixi180 – 1823Combined sources
Beta strandi184 – 1918Combined sources
Helixi197 – 1993Combined sources
Beta strandi202 – 2043Combined sources
Helixi205 – 21511Combined sources
Helixi224 – 23512Combined sources
Helixi237 – 2393Combined sources
Beta strandi246 – 2505Combined sources
Helixi253 – 2553Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OIFX-ray2.60A/B/C/D1-258[»]
3OIGX-ray1.25A1-258[»]
ProteinModelPortaliP54616.
SMRiP54616. Positions 1-258.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54616.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0623.
InParanoidiP54616.
KOiK00208.
OMAiTGEIHHV.
OrthoDBiEOG6HF644.
PhylomeDBiP54616.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR014358. Enoyl-ACP_Rdtase_NADH.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PIRSFiPIRSF000094. Enoyl-ACP_rdct. 1 hit.
PRINTSiPR00081. GDHRDH.

Sequencei

Sequence statusi: Complete.

P54616-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNFSLEGRNI VVMGVANKRS IAWGIARSLH EAGARLIFTY AGERLEKSVH
60 70 80 90 100
ELAGTLDRND SIILPCDVTN DAEIETCFAS IKEQVGVIHG IAHCIAFANK
110 120 130 140 150
EELVGEYLNT NRDGFLLAHN ISSYSLTAVV KAARPMMTEG GSIVTLTYLG
160 170 180 190 200
GELVMPNYNV MGVAKASLDA SVKYLAADLG KENIRVNSIS AGPIRTLSAK
210 220 230 240 250
GISDFNSILK DIEERAPLRR TTTPEEVGDT AAFLFSDMSR GITGENLHVD

SGFHITAR
Length:258
Mass (Da):27,874
Last modified:May 30, 2000 - v2
Checksum:i097667168B3F0470
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201S → Q AA sequence (PubMed:8755892)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13029.2.
PIRiG69845.
RefSeqiNP_389054.2. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB13029; CAB13029; BSU11720.
GeneIDi939379.
KEGGibsu:BSU11720.
PATRICi18974061. VBIBacSub10457_1224.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13029.2 .
PIRi G69845.
RefSeqi NP_389054.2. NC_000964.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali P54616.
SMRi P54616. Positions 1-258.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P54616. 1 interaction.
MINTi MINT-8366040.
STRINGi 224308.BSU11720.

Chemistry

BindingDBi P54616.
ChEMBLi CHEMBL1075044.

Proteomic databases

PaxDbi P54616.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB13029 ; CAB13029 ; BSU11720 .
GeneIDi 939379.
KEGGi bsu:BSU11720.
PATRICi 18974061. VBIBacSub10457_1224.

Organism-specific databases

GenoListi BSU11720. [Micado ]

Phylogenomic databases

eggNOGi COG0623.
InParanoidi P54616.
KOi K00208.
OMAi TGEIHHV.
OrthoDBi EOG6HF644.
PhylomeDBi P54616.

Enzyme and pathway databases

UniPathwayi UPA00094 .
BioCyci BSUB:BSU11720-MONOMER.
SABIO-RK P54616.

Miscellaneous databases

EvolutionaryTracei P54616.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR014358. Enoyl-ACP_Rdtase_NADH.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PIRSFi PIRSF000094. Enoyl-ACP_rdct. 1 hit.
PRINTSi PR00081. GDHRDH.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiFABI_BACSU
AccessioniPrimary (citable) accession number: P54616
Secondary accession number(s): O31621
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 30, 2000
Last modified: November 26, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3