FABF_RHIME
ID FABF_RHIME Reviewed; 421 AA.
AC P56902;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 25-MAY-2022, entry version 118.
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; OrderedLocusNames=R01144; ORFNames=SMc00574;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=10784042; DOI=10.1099/00221287-146-4-839;
RA Lopez-Lara I.M., Geiger O.;
RT "Expression and purification of four different rhizobial acyl carrier
RT proteins.";
RL Microbiology 146:839-849(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
CC -!- FUNCTION: Involved in the type II fatty acid elongation cycle.
CC Catalyzes the elongation of a wide range of acyl-ACP by the addition of
CC two carbons from malonyl-ACP to an acyl acceptor. Can efficiently
CC catalyze the conversion of palmitoleoyl-ACP (cis-hexadec-9-enoyl-ACP)
CC to cis-vaccenoyl-ACP (cis-octadec-11-enoyl-ACP), an essential step in
CC the thermal regulation of fatty acid composition.
CC {ECO:0000250|UniProtKB:P0AAI5}.
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 -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:P0AAI5}.
CC -!- SUBUNIT: Homodimer. {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; AF159244; AAF24182.2; -; Genomic_DNA.
DR EMBL; AL591688; CAC45723.1; -; Genomic_DNA.
DR RefSeq; NP_385250.1; NC_003047.1.
DR RefSeq; WP_010969069.1; NC_003047.1.
DR AlphaFoldDB; P56902; -.
DR SMR; P56902; -.
DR STRING; 266834.SMc00574; -.
DR EnsemblBacteria; CAC45723; CAC45723; SMc00574.
DR GeneID; 61602603; -.
DR KEGG; sme:SMc00574; -.
DR PATRIC; fig|266834.11.peg.2553; -.
DR eggNOG; COG0304; Bacteria.
DR HOGENOM; CLU_000022_69_2_5; -.
DR OMA; QIGHCLG; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001976; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW Acyltransferase; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..421
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 2"
FT /id="PRO_0000180317"
FT ACT_SITE 170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
SQ SEQUENCE 421 AA; 44263 MW; CBAAA634A5AD08CF CRC64;
MRRVVITGTG MVSPLGCGTE VSWARLLTGD NAARKVTEFE VEDLPAKIAC RIPFGDGSDG
TFNADDWMEP KEQRKVDPFI VYAMAAADMA LADAGWKPES DEDQISTGVL IGSGIGGLEG
IVDAGYTLRD KGPRRISPFF IPGRLINLAA GQVSIRHKLR GPNHSVVTAC STGAHAIGDA
SRLIALGDAD VMVAGGTESP ICRISLAGFA ACKALSTQHN DNPEKASRPY DADRDGFVMG
EGAGIVVLEE LEHARARGAK IYAEVIGYGL SGDAFHITAP SEDGEGAYRC MQMALKRAGV
TAADIDYINA HGTSTMADTI ELGAVERLVG DSASRISMSS TKSAIGHLLG AAGAVEAIFS
ALAIRDNIAP PTLNLDNPSV ETKIDLVPHV ARKREINVAL SNSFGFGGTN ASLILRRYTG
H
