FABL_BACSU
ID FABL_BACSU Reviewed; 250 AA.
AC P71079; Q796Z2;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADPH] FabL;
DE Short=ENR;
DE EC=1.3.1.104;
DE AltName: Full=Enoyl-acyl carrier protein reductase III;
DE AltName: Full=NADPH-dependent enoyl-ACP reductase;
GN Name=fabL; Synonyms=yfhR, ygaA; OrderedLocusNames=BSU08650;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8946165; DOI=10.1093/dnares/3.4.257;
RA Yamamoto H., Uchiyama S., Sekiguchi J.;
RT "Cloning and sequencing of a 27.8-kb nucleotide sequence of the 79 degrees-
RT 81 degrees region of the Bacillus subtilis genome containing the sspE
RT locus.";
RL DNA Res. 3:257-262(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9202460; DOI=10.1099/00221287-143-6-1855;
RA Cummings N.J., Connerton I.F.;
RT "The Bacillus subtilis 168 chromosome from sspE to katA.";
RL Microbiology 143:1855-1859(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP INDUCTION.
RC STRAIN=168;
RX PubMed=10463184; DOI=10.1099/13500872-145-8-2171;
RA Yamamoto H., Mori M., Sekiguchi J.;
RT "Transcription of genes near the sspE locus of the Bacillus subtilis
RT genome.";
RL Microbiology 145:2171-2180(1999).
RN [5]
RP FUNCTION AS AN ENOYL-ACP REDUCTASE AND IN FATTY ACID BIOSYNTHESIS,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE,
RP AND ACTIVITY REGULATION.
RX PubMed=11007778; DOI=10.1074/jbc.m005611200;
RA Heath R.J., Su N., Murphy C.K., Rock C.O.;
RT "The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus
RT subtilis.";
RL J. Biol. Chem. 275:40128-40133(2000).
RN [6]
RP CRYSTALLIZATION.
RC STRAIN=168;
RX PubMed=17329825; DOI=10.1107/s1744309107008469;
RA Kim K.-H., Park J.K., Ha B.H., Moon J.H., Kim E.E.;
RT "Crystallization and preliminary X-ray crystallographic analysis of enoyl-
RT ACP reductase III (FabL) from Bacillus subtilis.";
RL Acta Crystallogr. F 63:246-248(2007).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH NADP AND INHIBITOR,
RP SUBUNIT, AND ACTIVE SITE.
RX PubMed=21185310; DOI=10.1016/j.jmb.2010.12.003;
RA Kim K.H., Ha B.H., Kim S.J., Hong S.K., Hwang K.Y., Kim E.E.;
RT "Crystal structures of Enoyl-ACP reductases I (FabI) and III (FabL) from B.
RT subtilis.";
RL J. Mol. Biol. 406:403-415(2011).
CC -!- FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an
CC enoyl moiety that is covalently linked to an acyl carrier protein
CC (ACP). It confers resistance to triclosan.
CC {ECO:0000269|PubMed:11007778}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-[ACP] + NADP(+) = a (2E)-enoyl-[ACP] +
CC H(+) + NADPH; Xref=Rhea:RHEA:22564, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.104;
CC Evidence={ECO:0000269|PubMed:11007778};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22566;
CC Evidence={ECO:0000269|PubMed:11007778};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-butenoyl-[ACP] + H(+) + NADPH = butanoyl-[ACP] + NADP(+);
CC Xref=Rhea:RHEA:41812, Rhea:RHEA-COMP:9627, Rhea:RHEA-COMP:9628,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78453, ChEBI:CHEBI:78454;
CC Evidence={ECO:0000269|PubMed:11007778};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41813;
CC Evidence={ECO:0000269|PubMed:11007778};
CC -!- ACTIVITY REGULATION: Inhibited by triclosan.
CC {ECO:0000269|PubMed:11007778}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16 uM for NADPH {ECO:0000269|PubMed:11007778};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:21185310}.
CC -!- INDUCTION: Expressed during exponential growth.
CC {ECO:0000269|PubMed:10463184}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene exhibit a 250-fold
CC decrease in the triclosan MIC. {ECO:0000269|PubMed:11007778}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; D85082; BAA24484.1; -; Genomic_DNA.
DR EMBL; Z82044; CAB04808.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12693.1; -; Genomic_DNA.
DR PIR; B69802; B69802.
DR RefSeq; NP_388745.1; NC_000964.3.
DR RefSeq; WP_003223262.1; NZ_JNCM01000032.1.
DR PDB; 3OIC; X-ray; 2.20 A; A/D=1-250.
DR PDB; 3OID; X-ray; 1.80 A; A/B/C/D=1-250.
DR PDBsum; 3OIC; -.
DR PDBsum; 3OID; -.
DR AlphaFoldDB; P71079; -.
DR SMR; P71079; -.
DR IntAct; P71079; 1.
DR MINT; P71079; -.
DR STRING; 224308.BSU08650; -.
DR SwissLipids; SLP:000001796; -.
DR jPOST; P71079; -.
DR PaxDb; P71079; -.
DR PRIDE; P71079; -.
DR EnsemblBacteria; CAB12693; CAB12693; BSU_08650.
DR GeneID; 64302718; -.
DR GeneID; 939223; -.
DR KEGG; bsu:BSU08650; -.
DR PATRIC; fig|224308.179.peg.933; -.
DR eggNOG; COG1028; Bacteria.
DR InParanoid; P71079; -.
DR OMA; VGTLGKQ; -.
DR PhylomeDB; P71079; -.
DR BioCyc; BSUB:BSU08650-MON; -.
DR BioCyc; MetaCyc:BSU08650-MON; -.
DR BRENDA; 1.3.1.10; 658.
DR BRENDA; 1.3.1.104; 658.
DR BRENDA; 1.3.1.39; 658.
DR SABIO-RK; P71079; -.
DR UniPathway; UPA00094; -.
DR EvolutionaryTrace; P71079; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IDA:UniProtKB.
DR GO; GO:0050661; F:NADP binding; IDA:UniProtKB.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0030497; P:fatty acid elongation; IDA:UniProtKB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..250
FT /note="Enoyl-[acyl-carrier-protein] reductase [NADPH] FabL"
FT /id="PRO_0000377006"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:21185310"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:21185310"
FT BINDING 13..16
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:21185310,
FT ECO:0007744|PDB:3OID"
FT BINDING 36..38
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:21185310,
FT ECO:0007744|PDB:3OID"
FT BINDING 62..63
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:21185310,
FT ECO:0007744|PDB:3OID"
FT BINDING 89
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:21185310,
FT ECO:0007744|PDB:3OID"
FT BINDING 158
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:21185310,
FT ECO:0007744|PDB:3OID"
FT BINDING 187..189
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:21185310,
FT ECO:0007744|PDB:3OID"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:3OID"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:3OID"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:3OID"
FT HELIX 39..50
FT /evidence="ECO:0007829|PDB:3OID"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:3OID"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:3OID"
FT HELIX 66..80
FT /evidence="ECO:0007829|PDB:3OID"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:3OID"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:3OID"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:3OID"
FT HELIX 115..129
FT /evidence="ECO:0007829|PDB:3OID"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:3OID"
FT STRAND 134..141
FT /evidence="ECO:0007829|PDB:3OID"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:3OID"
FT HELIX 152..171
FT /evidence="ECO:0007829|PDB:3OID"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:3OID"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:3OID"
FT HELIX 190..194
FT /evidence="ECO:0007829|PDB:3OID"
FT HELIX 198..208
FT /evidence="ECO:0007829|PDB:3OID"
FT HELIX 217..227
FT /evidence="ECO:0007829|PDB:3OID"
FT TURN 231..234
FT /evidence="ECO:0007829|PDB:3OID"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:3OID"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:3OID"
SQ SEQUENCE 250 AA; 27178 MW; 4314962C70E19C49 CRC64;
MEQNKCALVT GSSRGVGKAA AIRLAENGYN IVINYARSKK AALETAEEIE KLGVKVLVVK
ANVGQPAKIK EMFQQIDETF GRLDVFVNNA ASGVLRPVME LEETHWDWTM NINAKALLFC
AQEAAKLMEK NGGGHIVSIS SLGSIRYLEN YTTVGVSKAA LEALTRYLAV ELSPKQIIVN
AVSGGAIDTD ALKHFPNRED LLEDARQNTP AGRMVEIKDM VDTVEFLVSS KADMIRGQTI
IVDGGRSLLV
