ID K9QCE1_9NOSO Unreviewed; 415 AA.
AC K9QCE1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 2 {ECO:0000256|ARBA:ARBA00014657, ECO:0000256|PIRNR:PIRNR000447};
DE EC=2.3.1.179 {ECO:0000256|ARBA:ARBA00012356, ECO:0000256|PIRNR:PIRNR000447};
GN ORFNames=Nos7107_2720 {ECO:0000313|EMBL:AFY43320.1};
OS Nostoc sp. PCC 7107.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=317936 {ECO:0000313|EMBL:AFY43320.1, ECO:0000313|Proteomes:UP000010381};
RN [1] {ECO:0000313|EMBL:AFY43320.1, ECO:0000313|Proteomes:UP000010381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7107 {ECO:0000313|EMBL:AFY43320.1,
RC ECO:0000313|Proteomes:UP000010381};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished genome of Nostoc sp. PCC 7107.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|PIRNR:PIRNR000447}.
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:0000256|PIRNR:PIRNR000447};
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:0000256|PIRNR:PIRNR000447};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194, ECO:0000256|PIRNR:PIRNR000447}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000256|ARBA:ARBA00008467,
CC ECO:0000256|PIRNR:PIRNR000447, ECO:0000256|RuleBase:RU003694}.
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DR EMBL; CP003548; AFY43320.1; -; Genomic_DNA.
DR RefSeq; WP_015113533.1; NC_019676.1.
DR AlphaFoldDB; K9QCE1; -.
DR STRING; 317936.Nos7107_2720; -.
DR KEGG; nos:Nos7107_2720; -.
DR PATRIC; fig|317936.3.peg.2954; -.
DR eggNOG; COG0304; Bacteria.
DR HOGENOM; CLU_000022_69_2_3; -.
DR InParanoid; K9QCE1; -.
DR OrthoDB; 9808669at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000010381; 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; -; 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 NCBIfam; TIGR03150; fabF; 1.
DR PANTHER; PTHR11712:SF336; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11712; POLYKETIDE SYNTHASE-RELATED; 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; Thiolase-like; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|PIRNR:PIRNR000447};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160,
KW ECO:0000256|PIRNR:PIRNR000447};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW ECO:0000256|PIRNR:PIRNR000447};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000010381};
KW Transferase {ECO:0000256|PIRNR:PIRNR000447, ECO:0000256|RuleBase:RU003694}.
FT DOMAIN 6..414
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT ACT_SITE 167
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000447-1"
SQ SEQUENCE 415 AA; 43766 MW; FA077CF860CCD02D CRC64;
MTDYIRKRVV VTGVGAITPI GNTPAEYWQG LISGRNGIDY ITHFDASSHD CRIAGEVKNF
DPHDYLERKE VKRMDRFSQF GVSAAKQALA DANLVINELN AEQVGVIIGS GIGGIKVLED
QQTIYLNRGP DRCSPFMIPM MIANMAAGLT AIHTGAKGPN NCTVTACAAG SNAIGDAFRL
IQGGYAQAMI CGGCEAAITP LSVAGFAACK ALSFRNDDPA HACRPFDRDR DGFVMGEGAG
ILILEELQHA LSRGARIYGE IVGYGMTCDA YHMTSPVPGG EGAARAIQLA LKDAGITPEQ
VTYVNAHGTS TPANDSNETS AIKTALGDHA YKIAVSSTKS MTGHLLGGSG GIEAVATVLA
IANEKIPPTI NLENPDAACD LDYVPHTSRA QKIEVALSNS FGFGGHNVTL VFKKY
//
