ID R9GUF3_9SPHI Unreviewed; 409 AA.
AC R9GUF3;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=ADIARSV_1306 {ECO:0000313|EMBL:EOR95487.1};
OS Arcticibacter svalbardensis MN12-7.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Arcticibacter.
OX NCBI_TaxID=1150600 {ECO:0000313|EMBL:EOR95487.1, ECO:0000313|Proteomes:UP000014174};
RN [1] {ECO:0000313|EMBL:EOR95487.1, ECO:0000313|Proteomes:UP000014174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MN12-7 {ECO:0000313|EMBL:EOR95487.1,
RC ECO:0000313|Proteomes:UP000014174};
RX PubMed=23846277;
RA Shivaji S., Ara S., Prasad S., Manasa B.P., Begum Z., Singh A.,
RA Kumar Pinnaka A.;
RT "Draft Genome Sequence of Arcticibacter svalbardensis Strain MN12-7T, a
RT Member of the Family Sphingobacteriaceae Isolated from an Arctic Soil
RT Sample.";
RL Genome Announc. 1:E00484-13(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOR95487.1}.
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DR EMBL; AQPN01000049; EOR95487.1; -; Genomic_DNA.
DR AlphaFoldDB; R9GUF3; -.
DR STRING; 1150600.ADIARSV_1306; -.
DR PATRIC; fig|1150600.3.peg.1283; -.
DR eggNOG; COG0304; Bacteria.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000014174; Unassembled WGS sequence.
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:UP000014174};
KW Transferase {ECO:0000256|PIRNR:PIRNR000447, ECO:0000256|RuleBase:RU003694}.
FT DOMAIN 1..408
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT ACT_SITE 159
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000447-1"
SQ SEQUENCE 409 AA; 43716 MW; 6E6252646EB29089 CRC64;
MITGLGALTP LGNNIATFWE NIIAGKSGAA RITRFDPSLF RTQFACELKD FNAADFLDRT
EIKRTDPFTQ YALVASDEAI KDSGFDLNKM DPFDVGVIWG TGQGGMETFE EQVEAYALGD
GHPRFSPFFV PKLIANMSSG MISIRNGYMG INYTTVSACA TSNTAIMDAY NYIRLGKAKI
IITGGSEAPI TAASVGGFSS MKAMSTQNDA PEQASRPFDV DRDGFVMAEG AGALVLEDYE
HAISRGAHIY GELTGAAMTS DAYHMTSTHP EGIGAAKAMQ LALQEAGISI NEVDYLNMHA
TSTHVGDISE IKALLSLTGN NKTNMMISAT KSMTGHLLGA AGAIEAIICL LSIRDQVIPP
TINTENLDPI IPESLNIVLK ETIDHKVKVA MSNTFGFGGH NGIVLFQSL
//
