ID C3ZBB7_BRAFL Unreviewed; 336 AA.
AC C3ZBB7;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Malonyl-CoA:ACP transacylase (MAT) domain-containing protein {ECO:0000259|SMART:SM00827};
DE Flags: Fragment;
GN ORFNames=BRAFLDRAFT_211460 {ECO:0000313|EMBL:EEN50154.1};
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:EEN50154.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN50154.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN50154.1};
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};
CC -!- SIMILARITY: Belongs to the FabD family.
CC {ECO:0000256|ARBA:ARBA00008217}.
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DR EMBL; GG666603; EEN50154.1; -; Genomic_DNA.
DR RefSeq; XP_002594143.1; XM_002594097.1.
DR AlphaFoldDB; C3ZBB7; -.
DR STRING; 7739.C3ZBB7; -.
DR eggNOG; KOG2926; Eukaryota.
DR InParanoid; C3ZBB7; -.
DR UniPathway; UPA00094; -.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR024925; Malonyl_CoA-ACP_transAc.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR PANTHER; PTHR47170; MALONYL-COA ACP TRANSACYLASE, ACP-BINDING; 1.
DR PANTHER; PTHR47170:SF2; PKS_AT DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR PIRSF; PIRSF000446; Mct; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
PE 3: Inferred from homology;
FT DOMAIN 11..335
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EEN50154.1"
SQ SEQUENCE 336 AA; 37412 MW; 9088337085643BBD CRC64;
RKDPRKSTVF LFPGQGAQFV GMARSLLDYP HVEDIFTRAR DILGYDILQL CLNGPQEELN
KTVHCQPAVF LTSLAAVERL REDNPLAMET CVAAAGFSVG EYAALVFSGA ISFEEALYVV
KERAAAMQRA SEEVPSGMLS VLGRPQTRFP QLCHDARIYC KEVHNMEDPV CSIANYLYPQ
ARVIGGNKEC LAYIRKYGKE YGLVRMKPVP VSGAFHTSLM ESAQDATHKA LQEVDIEVPV
INVHSNVDTA SYQNPQQMRR LLTKQVTSPV KWEQLMHTLY ERPQGRGFPD TFEVGPGSQL
GAVLSRCNMK ARQEYRKVSC GEEDDNTSSV QATAND
//
