FABF_SYNY3
ID FABF_SYNY3 Reviewed; 416 AA.
AC P73283;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 137.
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=sll1069;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2] {ECO:0007744|PDB:1E5M}
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS), AND SUBUNIT.
RX PubMed=11152607; DOI=10.1006/jmbi.2000.4272;
RA Moche M., Dehesh K., Edwards P., Lindqvist Y.;
RT "The crystal structure of beta-ketoacyl-acyl carrier protein synthase II
RT from Synechocystis sp. at 1.54 A resolution and its relationship to other
RT condensing enzymes.";
RL J. Mol. Biol. 305:491-503(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:0000269|PubMed:11152607}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000305}.
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DR EMBL; BA000022; BAA17311.1; -; Genomic_DNA.
DR PIR; S77464; S77464.
DR PDB; 1E5M; X-ray; 1.54 A; A=1-416.
DR PDBsum; 1E5M; -.
DR AlphaFoldDB; P73283; -.
DR SMR; P73283; -.
DR STRING; 1148.1652389; -.
DR PaxDb; P73283; -.
DR EnsemblBacteria; BAA17311; BAA17311; BAA17311.
DR KEGG; syn:sll1069; -.
DR eggNOG; COG0304; Bacteria.
DR InParanoid; P73283; -.
DR OMA; QIGHCLG; -.
DR PhylomeDB; P73283; -.
DR BRENDA; 2.3.1.179; 382.
DR UniPathway; UPA00094; -.
DR EvolutionaryTrace; P73283; -.
DR Proteomes; UP000001425; 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 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..416
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 2"
FT /id="PRO_0000180326"
FT ACT_SITE 167
FT STRAND 9..18
FT /evidence="ECO:0007829|PDB:1E5M"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:1E5M"
FT HELIX 24..32
FT /evidence="ECO:0007829|PDB:1E5M"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1E5M"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1E5M"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:1E5M"
FT HELIX 68..72
FT /evidence="ECO:0007829|PDB:1E5M"
FT HELIX 76..92
FT /evidence="ECO:0007829|PDB:1E5M"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:1E5M"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:1E5M"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:1E5M"
FT HELIX 115..128
FT /evidence="ECO:0007829|PDB:1E5M"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:1E5M"
FT HELIX 137..141
FT /evidence="ECO:0007829|PDB:1E5M"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:1E5M"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:1E5M"
FT HELIX 169..182
FT /evidence="ECO:0007829|PDB:1E5M"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:1E5M"
FT HELIX 200..208
FT /evidence="ECO:0007829|PDB:1E5M"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:1E5M"
FT STRAND 238..246
FT /evidence="ECO:0007829|PDB:1E5M"
FT HELIX 247..252
FT /evidence="ECO:0007829|PDB:1E5M"
FT STRAND 259..268
FT /evidence="ECO:0007829|PDB:1E5M"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:1E5M"
FT HELIX 281..294
FT /evidence="ECO:0007829|PDB:1E5M"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:1E5M"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:1E5M"
FT HELIX 312..326
FT /evidence="ECO:0007829|PDB:1E5M"
FT HELIX 327..332
FT /evidence="ECO:0007829|PDB:1E5M"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:1E5M"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:1E5M"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:1E5M"
FT HELIX 349..363
FT /evidence="ECO:0007829|PDB:1E5M"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:1E5M"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:1E5M"
FT STRAND 394..402
FT /evidence="ECO:0007829|PDB:1E5M"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:1E5M"
FT STRAND 406..413
FT /evidence="ECO:0007829|PDB:1E5M"
SQ SEQUENCE 416 AA; 44004 MW; B0740A438A91A6C1 CRC64;
MANLEKKRVV VTGLGAITPI GNTLQDYWQG LMEGRNGIGP ITRFDASDQA CRFGGEVKDF
DATQFLDRKE AKRMDRFCHF AVCASQQAIN DAKLVINELN ADEIGVLIGT GIGGLKVLED
QQTILLDKGP SRCSPFMIPM MIANMASGLT AINLGAKGPN NCTVTACAAG SNAIGDAFRL
VQNGYAKAMI CGGTEAAITP LSYAGFASAR ALSFRNDDPL HASRPFDKDR DGFVMGEGSG
ILILEELESA LARGAKIYGE MVGYAMTCDA YHITAPVPDG RGATRAIAWA LKDSGLKPEM
VSYINAHGTS TPANDVTETR AIKQALGNHA YNIAVSSTKS MTGHLLGGSG GIEAVATVMA
IAEDKVPPTI NLENPDPECD LDYVPGQSRA LIVDVALSNS FGFGGHNVTL AFKKYQ
