FABF_BACSU
ID FABF_BACSU Reviewed; 413 AA.
AC O34340;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 2;
DE EC=2.3.1.179 {ECO:0000250|UniProtKB:P0AAI5};
DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase II;
DE AltName: Full=Beta-ketoacyl-ACP synthase II;
DE Short=KAS II;
GN Name=fabF {ECO:0000303|PubMed:11325930}; Synonyms=yjaY;
GN OrderedLocusNames=BSU11340;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP FUNCTION, ACTIVITY REGULATION, AND VARIANT PHE-109.
RC STRAIN=168 / JH642;
RX PubMed=11325930; DOI=10.1128/jb.183.10.3032-3040.2001;
RA Schujman G.E., Choi K.H., Altabe S., Rock C.O., de Mendoza D.;
RT "Response of Bacillus subtilis to cerulenin and acquisition of
RT resistance.";
RL J. Bacteriol. 183:3032-3040(2001).
CC -!- FUNCTION: Involved in the type II fatty acid elongation cycle
CC (PubMed:11325930). Catalyzes the elongation of a wide range of acyl-ACP
CC by the addition of two carbons from malonyl-ACP to an acyl acceptor
CC (PubMed:11325930). Can efficiently catalyze the conversion of
CC palmitoleoyl-ACP (cis-hexadec-9-enoyl-ACP) to cis-vaccenoyl-ACP (cis-
CC octadec-11-enoyl-ACP), an essential step in the thermal regulation of
CC fatty acid composition (By similarity). {ECO:0000250|UniProtKB:P0AAI5,
CC ECO:0000269|PubMed:11325930}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP]
CC + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
CC Evidence={ECO:0000250|UniProtKB:P0AAI5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(11Z)-
CC octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:55040,
CC Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:10800,
CC Rhea:RHEA-COMP:14074, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:83989,
CC ChEBI:CHEBI:138538; EC=2.3.1.179;
CC Evidence={ECO:0000250|UniProtKB:P0AAI5};
CC -!- ACTIVITY REGULATION: Inhibited by cerulenin.
CC {ECO:0000269|PubMed:11325930}.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:P0AAI5}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000305}.
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DR EMBL; AL009126; CAB12975.1; -; Genomic_DNA.
DR PIR; G69842; G69842.
DR RefSeq; NP_389016.1; NC_000964.3.
DR RefSeq; WP_003244890.1; NZ_JNCM01000035.1.
DR PDB; 4LS5; X-ray; 1.80 A; A/B=1-413.
DR PDB; 4LS6; X-ray; 1.56 A; A/B=1-413.
DR PDB; 4LS7; X-ray; 1.67 A; A/B=1-413.
DR PDB; 4LS8; X-ray; 2.10 A; A/B=1-413.
DR PDBsum; 4LS5; -.
DR PDBsum; 4LS6; -.
DR PDBsum; 4LS7; -.
DR PDBsum; 4LS8; -.
DR AlphaFoldDB; O34340; -.
DR SMR; O34340; -.
DR MINT; O34340; -.
DR STRING; 224308.BSU11340; -.
DR jPOST; O34340; -.
DR PaxDb; O34340; -.
DR PRIDE; O34340; -.
DR EnsemblBacteria; CAB12975; CAB12975; BSU_11340.
DR GeneID; 939803; -.
DR KEGG; bsu:BSU11340; -.
DR PATRIC; fig|224308.179.peg.1219; -.
DR eggNOG; COG0304; Bacteria.
DR InParanoid; O34340; -.
DR OMA; YRYIKYK; -.
DR PhylomeDB; O34340; -.
DR BioCyc; BSUB:BSU11340-MON; -.
DR BioCyc; MetaCyc:BSU11340-MON; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR CDD; cd00834; KAS_I_II; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR017568; 3-oxoacyl-ACP_synth-2.
DR InterPro; IPR000794; Beta-ketoacyl_synthase.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR11712; PTHR11712; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR PIRSF; PIRSF000447; KAS_II; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR03150; fabF; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
KW Reference proteome; Transferase.
FT CHAIN 1..413
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 2"
FT /id="PRO_0000360846"
FT ACT_SITE 164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT VARIANT 109
FT /note="I -> F (in strain: GS77; resistant to cerulenin)"
FT /evidence="ECO:0000269|PubMed:11325930"
FT STRAND 6..15
FT /evidence="ECO:0007829|PDB:4LS6"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:4LS6"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:4LS6"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:4LS6"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:4LS6"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:4LS6"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:4LS6"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:4LS6"
FT HELIX 73..89
FT /evidence="ECO:0007829|PDB:4LS6"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:4LS6"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:4LS6"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:4LS6"
FT HELIX 112..125
FT /evidence="ECO:0007829|PDB:4LS6"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:4LS6"
FT HELIX 134..138
FT /evidence="ECO:0007829|PDB:4LS6"
FT HELIX 142..151
FT /evidence="ECO:0007829|PDB:4LS6"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:4LS6"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:4LS6"
FT HELIX 166..179
FT /evidence="ECO:0007829|PDB:4LS6"
FT STRAND 184..192
FT /evidence="ECO:0007829|PDB:4LS6"
FT HELIX 197..205
FT /evidence="ECO:0007829|PDB:4LS6"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:4LS6"
FT STRAND 234..242
FT /evidence="ECO:0007829|PDB:4LS6"
FT HELIX 243..248
FT /evidence="ECO:0007829|PDB:4LS6"
FT STRAND 255..264
FT /evidence="ECO:0007829|PDB:4LS6"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:4LS6"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:4LS6"
FT HELIX 277..290
FT /evidence="ECO:0007829|PDB:4LS6"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:4LS6"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:4LS6"
FT HELIX 308..322
FT /evidence="ECO:0007829|PDB:4LS6"
FT HELIX 323..327
FT /evidence="ECO:0007829|PDB:4LS6"
FT STRAND 329..332
FT /evidence="ECO:0007829|PDB:4LS6"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:4LS6"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:4LS6"
FT HELIX 345..359
FT /evidence="ECO:0007829|PDB:4LS6"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:4LS6"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:4LS6"
FT STRAND 390..398
FT /evidence="ECO:0007829|PDB:4LS6"
FT TURN 399..401
FT /evidence="ECO:0007829|PDB:4LS6"
FT STRAND 402..409
FT /evidence="ECO:0007829|PDB:4LS6"
SQ SEQUENCE 413 AA; 44005 MW; 4667233C9E855740 CRC64;
MTKKRVVVTG LGALSPLGND VDTSWNNAIN GVSGIGPITR VDAEEYPAKV AAELKDFNVE
DYMDKKEARK MDRFTQYAVV AAKMAVEDAD LNITDEIAPR VGVWVGSGIG GLETLESQFE
IFLTKGPRRV SPFFVPMMIP DMATGQISIA LGAKGVNSCT VTACATGTNS IGDAFKVIQR
GDADVMVTGG TEAPLTRMSF AGFSANKALS TNPDPKTASR PFDKNRDGFV MGEGAGIIVL
EELEHALARG AKIYGEIVGY GSTGDAYHIT APAQDGEGGA RAMQEAIKDA GIAPEEIDYI
NAHGTSTYYN DKYETMAIKT VFGEHAHKLA VSSTKSMTGH LLGAAGGIEA IFSILAIKEG
VIPPTINIQT PDEECDLDYV PDEARRQELN YVLSNSLGFG GHNATLIFKK YQS
