ID C3XS41_BRAFL Unreviewed; 1503 AA.
AC C3XS41;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Ketosynthase family 3 (KS3) domain-containing protein {ECO:0000259|PROSITE:PS52004};
GN ORFNames=BRAFLDRAFT_71890 {ECO:0000313|EMBL:EEN69509.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN69509.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN69509.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN69509.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
CC Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449; EC=2.3.1.39;
CC Evidence={ECO:0000256|ARBA:ARBA00023404};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41793;
CC Evidence={ECO:0000256|ARBA:ARBA00023404};
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DR EMBL; GG666456; EEN69509.1; -; Genomic_DNA.
DR RefSeq; XP_002613500.1; XM_002613454.1.
DR STRING; 7739.C3XS41; -.
DR eggNOG; KOG1202; Eukaryota.
DR InParanoid; C3XS41; -.
DR UniPathway; UPA00094; -.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
FT DOMAIN 2..122
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 1503 AA; 166895 MW; 713E4F586BB3C24B CRC64;
MDEKVAIVGI GCRYPGGVNT PGDFWTMLAE GRDCTIPPPD DRFDTSYFWH PNRTPGKLYN
RCGGYLQCNV FEFDRQFFKI PPDEANHLDP QIQLLLEVTW EALENAGIPS RSIRGSNTGV
YVDIHFDALN IQVPSNLLQW EEKGNRLAGC SSFGFGGANA HLILERSPLP DLHPAVNNSD
KVNDNHFTVG TGHETAKTIM LLSGNSKAAL KEQIKHWISF ITDTPTLNED RFQQSLYTSA
NRYQHHAERL AIVVNGADDA VQKLDLMARE EKLSAVVEGK VPEGAERGKM AFVFSGMGTQ
WWGMGRKLAQ EDPVFRDVIQ RFEDVLKTLG ADWSIADMLT KETNPDKINR TDIAQPCICA
VQMGLVELLK QYDVIPDAIV GHSVGEVAAA YAAGLLSFED AVRVIYHRGK ELSKTSGHGK
MLAVLHPMEE VEKLVERDEN RNIINVAATN SPNQIVLSGD GAAIDSFHNK LKSKGIKCVL
LKVNNAFHSY QQEQVKDSIL NKLRILSASS RTTKAQIPII STVTNQWLSS DITNTAHYWW
TNIRQQVRFM QSVQVLLREG YSTFVEIGAH PALGPALKDI SSTSKSRTTK QNIIPTLIRP
KDTSSPADDR ENILVATGTL HVVGYPVNFS PAFQEKHRGV HDIPTYPWQR VLCNAGTERS
SSRYQFPQRA HPLLGQAQET AEGTKSQKSK IWCSHLSEES VPWLKHHILD GNVVVPAAAY
VETALAAASD IYGDQNVLSL KNLQFKRFMF APTSEAEMKS TVQHRSAKEK HFDLYSKDAS
GSWILHATAE VHKGDLKQQV GSTNVLTNVA ERCSKTISSE EIYEAAEEAG FHLGSSFHCV
TSCTTSDNYE EAVVTAEAPE EISREFGRYI YHPAFMDTFL HTFACLSLLN DKYTGKTPAK
RVPFSMKSLY MFNKMPSKVN LYFRISKRGS RRVVDITVTD SSGHEIVCEV EELMFEDIDT
GSSSGIKLWN LQWEPLVKND SNEDKKPTAY KHVLVIHEDE DESFGTTVST ALQTNLGCTV
EMMNQNILTE DEGSEKMLTH DDLDHVIVLY DSVSQEQTGG SGGCPFAEVL RSYKCLSTFK
RISQLDHPPT LWIFTRGSSS VLEQDTVSPL LAGTSSLCLS ITQEYPQLKV KAVDLTPQLN
FVDAAAEVLS VLKANPRENE IAARMVNSPD DKQVNLYARR LNPMKPDQIL TSCSPKESWV
FDSKQRHNGK KLYKAQSSPS TPMGNEATVK VAAFAVYPFS DLFGSSDGPA HDIHLIYGTV
HHSPTNMVVR HIPTDMMVQE GSRVMGVVMG CISPQMNIQM RNLVPLPGTL SWDDAVAIVK
DFLPAFSFFQ KIQTVCKEDR VVVFLPDEDD RETLSYATLA LQQQAEVCVV ADTGQNGDIE
KRIFCTTGSR PPTSSTVIST YDKLDQDIPD KHASVAFLPK GDRAGEVLQQ AARKLQAFGT
LVNLGGSTIL MDQLPKNIKF ITVDPLDSPQ GDSSLSCMAT PYKYRFHLQV VNGGHRDALI
SEL
//
