FABF_VIBCH
ID FABF_VIBCH Reviewed; 414 AA.
AC Q9KQH9;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-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=VC_2019;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2] {ECO:0007744|PDB:4JRH, ECO:0007744|PDB:4JRM}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RA Hou J., Chruszcz M., Shabalin I.G., Zheng H., Cooper D.R., Anderson W.F.,
RA Minor W.;
RT "Crystal structure of beta-ketoacyl-ACP synthase II (FabF) from Vibrio
RT cholerae (space group P43) at 2.2 Angstrom.";
RL Submitted (MAR-2013) to the PDB data bank.
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; AE003852; AAF95167.1; -; Genomic_DNA.
DR PIR; D82128; D82128.
DR RefSeq; NP_231653.1; NC_002505.1.
DR RefSeq; WP_000044695.1; NZ_LT906614.1.
DR PDB; 4JRH; X-ray; 2.20 A; A/B=1-414.
DR PDB; 4JRM; X-ray; 1.75 A; A/B/C/D=1-414.
DR PDBsum; 4JRH; -.
DR PDBsum; 4JRM; -.
DR AlphaFoldDB; Q9KQH9; -.
DR SMR; Q9KQH9; -.
DR STRING; 243277.VC_2019; -.
DR DNASU; 2613398; -.
DR EnsemblBacteria; AAF95167; AAF95167; VC_2019.
DR GeneID; 57740640; -.
DR GeneID; 66940449; -.
DR KEGG; vch:VC_2019; -.
DR PATRIC; fig|243277.26.peg.1929; -.
DR eggNOG; COG0304; Bacteria.
DR HOGENOM; CLU_000022_69_2_6; -.
DR OMA; QIGHCLG; -.
DR BioCyc; VCHO:VC2019-MON; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000584; Chromosome 1.
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; -; 1.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..414
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 2"
FT /id="PRO_0000180327"
FT ACT_SITE 164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT STRAND 6..15
FT /evidence="ECO:0007829|PDB:4JRM"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:4JRM"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:4JRM"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:4JRM"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:4JRM"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:4JRM"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:4JRM"
FT HELIX 73..89
FT /evidence="ECO:0007829|PDB:4JRM"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:4JRM"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:4JRM"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:4JRM"
FT HELIX 112..125
FT /evidence="ECO:0007829|PDB:4JRM"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:4JRM"
FT HELIX 134..138
FT /evidence="ECO:0007829|PDB:4JRM"
FT HELIX 142..151
FT /evidence="ECO:0007829|PDB:4JRM"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:4JRM"
FT HELIX 166..180
FT /evidence="ECO:0007829|PDB:4JRM"
FT STRAND 184..192
FT /evidence="ECO:0007829|PDB:4JRM"
FT HELIX 197..205
FT /evidence="ECO:0007829|PDB:4JRM"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:4JRM"
FT STRAND 235..243
FT /evidence="ECO:0007829|PDB:4JRM"
FT HELIX 244..249
FT /evidence="ECO:0007829|PDB:4JRM"
FT STRAND 256..265
FT /evidence="ECO:0007829|PDB:4JRM"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:4JRM"
FT HELIX 278..291
FT /evidence="ECO:0007829|PDB:4JRM"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:4JRM"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:4JRM"
FT HELIX 309..330
FT /evidence="ECO:0007829|PDB:4JRM"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:4JRM"
FT HELIX 337..340
FT /evidence="ECO:0007829|PDB:4JRM"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:4JRM"
FT HELIX 347..361
FT /evidence="ECO:0007829|PDB:4JRM"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:4JRM"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:4JRM"
FT STRAND 394..401
FT /evidence="ECO:0007829|PDB:4JRM"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:4JRM"
FT STRAND 405..413
FT /evidence="ECO:0007829|PDB:4JRM"
SQ SEQUENCE 414 AA; 43208 MW; EB5942D01274ED1F CRC64;
MSKRRVVVTG MGMLSPVGNT VESSWKALLA GQSGIVNIEH FDTTNFSTRF AGLVKGFDCE
QYMSKKDARK MDLFIQYGIA AGIQALEDSG LEVNEENAAR IGVAIGSGIG GLELIETGHQ
ALIEKGPRKV SPFFVPSTIV NMIAGNLSIM RGLRGPNIAI STACTTGLHN IGHAARMIAY
GDADAMVAGG AEKASTPLGM AGFGAAKALS TRNDEPQKAS RPWDKDRDGF VLGDGAGIMV
LEEYEHAKAR GAKIYAEVVG FGMSGDAYHM TSPSEDGSGG ALAMEAAMRD AGVTGEQIGY
VNAHGTSTPA GDVAEVKGIK RALGEAGTKQ VLVSSTKSMT GHLLGAAGSV EAIITVMSLV
DQMVPPTINL DNPEEGLGVD LVPHVARKVE SMEYAMCNSF GFGGTNGSLI FKRM
