FABG_SYNY3
ID FABG_SYNY3 Reviewed; 247 AA.
AC P73574;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase {ECO:0000303|PubMed:26358291};
DE EC=1.1.1.100 {ECO:0000305|PubMed:26358291};
DE AltName: Full=3-ketoacyl-acyl carrier protein reductase;
GN Name=fabG; OrderedLocusNames=slr0886;
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:4RZH}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), FUNCTION, BIOTECHNOLOGY, AND
RP MUTAGENESIS OF ALA-14; PRO-151; LYS-160; PHE-188 AND ASN-198.
RX PubMed=26358291; DOI=10.1016/j.febslet.2015.09.001;
RA Liu Y., Feng Y., Cao X., Li X., Xue S.;
RT "Structure-directed construction of a high-performance version of the
RT enzyme FabG from the photosynthetic microorganism Synechocystis sp. PCC
RT 6803.";
RL FEBS Lett. 589:3052-3057(2015).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP
CC substrates to beta-hydroxyacyl-ACP products, the first reductive step
CC in the elongation cycle of fatty acid biosynthesis (Probable). Is
CC capable of reducing acetoacetyl-CoA, but less well than its paralog
CC PhaB (PubMed:26358291). {ECO:0000269|PubMed:26358291,
CC ECO:0000305|PubMed:26358291}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+)
CC + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
CC Evidence={ECO:0000305|PubMed:26358291};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- BIOTECHNOLOGY: Mutation of key residues to match those found in its
CC paralog PhaB increases it activity on acetoacetyl-CoA, not its usual
CC substrate, which might help shift cellular metabolism to make poly(3-
CC hydroxybutyrate) (PHB), a compound that has potential uses as a
CC renewable, biodegradable thermoplastic (PubMed:26358291). Poly(3-
CC hydroxyalkanoic acids) (PHA), of which PHB is among the most common
CC compounds, are prokaryotic intracellular storage compounds with
CC potential uses as a renewable, biodegradable thermoplastic.
CC Cyanobacterial PHB synthesis is particularly attractive as
CC cyanobacteria use CO(2) as the carbon source.
CC {ECO:0000269|PubMed:26358291}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; BA000022; BAA17614.1; -; Genomic_DNA.
DR PIR; S77280; S77280.
DR PDB; 4RZH; X-ray; 2.20 A; A/B=1-247.
DR PDBsum; 4RZH; -.
DR AlphaFoldDB; P73574; -.
DR SMR; P73574; -.
DR IntAct; P73574; 1.
DR STRING; 1148.1652694; -.
DR PaxDb; P73574; -.
DR EnsemblBacteria; BAA17614; BAA17614; BAA17614.
DR KEGG; syn:slr0886; -.
DR eggNOG; COG1028; Bacteria.
DR InParanoid; P73574; -.
DR OMA; KMPERDY; -.
DR PhylomeDB; P73574; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0030497; P:fatty acid elongation; IBA:GO_Central.
DR InterPro; IPR011284; 3oxo_ACP_reduc.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01830; 3oxo_ACP_reduc; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..247
FT /note="3-oxoacyl-[acyl-carrier-protein] reductase"
FT /id="PRO_0000054691"
FT ACT_SITE 156
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 11..35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MUTAGEN 14
FT /note="A->G: 4.2-fold increase in activity on acetoacetyl-
FT CoA."
FT /evidence="ECO:0000269|PubMed:26358291"
FT MUTAGEN 151
FT /note="P->F: 2.7-fold increase in activity on acetoacetyl-
FT CoA."
FT /evidence="ECO:0000269|PubMed:26358291"
FT MUTAGEN 151
FT /note="P->V: 5.7-fold increase in activity on acetoacetyl-
FT CoA."
FT /evidence="ECO:0000269|PubMed:26358291"
FT MUTAGEN 160
FT /note="K->A: Almost no activity on acetoacetyl-CoA."
FT /evidence="ECO:0000269|PubMed:26358291"
FT MUTAGEN 188
FT /note="F->Y: 3.3-fold increase in activity on acetoacetyl-
FT CoA."
FT /evidence="ECO:0000269|PubMed:26358291"
FT MUTAGEN 198
FT /note="N->R: 3.5-fold increase in activity on acetoacetyl-
FT CoA."
FT /evidence="ECO:0000269|PubMed:26358291"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:4RZH"
FT STRAND 8..13
FT /evidence="ECO:0007829|PDB:4RZH"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:4RZH"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:4RZH"
FT HELIX 41..53
FT /evidence="ECO:0007829|PDB:4RZH"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:4RZH"
FT HELIX 68..82
FT /evidence="ECO:0007829|PDB:4RZH"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:4RZH"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:4RZH"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:4RZH"
FT HELIX 117..132
FT /evidence="ECO:0007829|PDB:4RZH"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:4RZH"
FT HELIX 144..148
FT /evidence="ECO:0007829|PDB:4RZH"
FT HELIX 154..174
FT /evidence="ECO:0007829|PDB:4RZH"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:4RZH"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:4RZH"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:4RZH"
FT HELIX 214..226
FT /evidence="ECO:0007829|PDB:4RZH"
FT HELIX 228..232
FT /evidence="ECO:0007829|PDB:4RZH"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:4RZH"
SQ SEQUENCE 247 AA; 25724 MW; 91EBF9409C777F20 CRC64;
MTALTAQVAL VTGASRGIGK ATALALAATG MKVVVNYAQS STAADAVVAE IIANGGEAIA
VQANVANADE VDQLIKTTLD KFSRIDVLVN NAGITRDTLL LRMKLEDWQA VIDLNLTGVF
LCTKAVSKLM LKQKSGRIIN ITSVAGMMGN PGQANYSAAK AGVIGFTKTV AKELASRGVT
VNAVAPGFIA TDMTENLNAE PILQFIPLAR YGQPEEVAGT IRFLATDPAA AYITGQTFNV
DGGMVMF
