FABB_HAEIN
ID FABB_HAEIN Reviewed; 406 AA.
AC P43710;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 1 {ECO:0000250|UniProtKB:P0A953};
DE EC=2.3.1.41 {ECO:0000250|UniProtKB:P0A953};
DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase I {ECO:0000250|UniProtKB:P0A953};
DE AltName: Full=Beta-ketoacyl-ACP synthase I {ECO:0000250|UniProtKB:P0A953};
DE Short=KAS I {ECO:0000250|UniProtKB:P0A953};
GN Name=fabB; OrderedLocusNames=HI_1533;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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 also use
CC unsaturated fatty acids. Catalyzes a key reaction in unsaturated fatty
CC acid (UFA) synthesis, the elongation of the cis-3-decenoyl-ACP produced
CC by FabA. {ECO:0000250|UniProtKB:P0A953}.
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 EC=2.3.1.41; Evidence={ECO:0000250|UniProtKB:P0A953};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22837;
CC Evidence={ECO:0000250|UniProtKB:P0A953};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3Z)-decenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(5Z)-
CC dodecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:54940, Rhea:RHEA-
CC COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9927, Rhea:RHEA-
CC COMP:14042, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78798, ChEBI:CHEBI:138410;
CC Evidence={ECO:0000250|UniProtKB:P0A953};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54941;
CC Evidence={ECO:0000250|UniProtKB:P0A953};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:P0A953}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0A953}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A953}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000305}.
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DR EMBL; L42023; AAC23183.1; -; Genomic_DNA.
DR PIR; A64128; A64128.
DR RefSeq; NP_439682.1; NC_000907.1.
DR RefSeq; WP_005693560.1; NC_000907.1.
DR AlphaFoldDB; P43710; -.
DR SMR; P43710; -.
DR STRING; 71421.HI_1533; -.
DR EnsemblBacteria; AAC23183; AAC23183; HI_1533.
DR KEGG; hin:HI_1533; -.
DR PATRIC; fig|71421.8.peg.1604; -.
DR eggNOG; COG0304; Bacteria.
DR HOGENOM; CLU_000022_69_2_6; -.
DR OMA; YAYLSMQ; -.
DR PhylomeDB; P43710; -.
DR BioCyc; HINF71421:G1GJ1-1555-MON; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000579; 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; 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 SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..406
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 1"
FT /id="PRO_0000180313"
FT ACT_SITE 162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
SQ SEQUENCE 406 AA; 42649 MW; A17B8673156FDDAF CRC64;
MRRTVITGFG IISSIGNNKE EVLASLKAGK SGIEVVPEFV EMNMRSHVAG TIKLNPSEHI
DRKVFRFMGD AAAYAYLSMR EAIEDAGLTE DQVSNDRTGL VIGAGTGSAH NQLVACDAVR
GPRGVKAIGP YAVTKTMASS VSACLATPYK IRGVNYSMSS ACATSAHCIG HAVELIQLGK
QDVVFAGGAE ELSWECATEF DAMGAVSTKY NETPEKASRA YDANRDGFVI AGGGAVVVVE
ELEHALARGA KIYAEIVGYG ATSDGYDMVA PSGEGAERCM KQAMATVDTP IDYINVHGTS
TPVGDVKELG AIKNVFGDKI PAISSTKSMT GHSLGAAGAH EAIYTLLMLD NDFIAPSINI
ETLDEAAEGC NIVTETKENA GLQTVMSNSF GFGGTNATLI FKRYNG
