ID B8C2A9_THAPS Unreviewed; 356 AA.
AC B8C2A9;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Malonyl coa-acyl carrier protein transacylase {ECO:0000313|EMBL:EED92353.1};
DE EC=2.3.1.39 {ECO:0000313|EMBL:EED92353.1};
GN Name=MCT1 {ECO:0000313|EMBL:EED92353.1};
GN ORFNames=THAPSDRAFT_5219 {ECO:0000313|EMBL:EED92353.1};
OS Thalassiosira pseudonana (Marine diatom) (Cyclotella nana).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC Thalassiosiraceae; Thalassiosira.
OX NCBI_TaxID=35128 {ECO:0000313|EMBL:EED92353.1, ECO:0000313|Proteomes:UP000001449};
RN [1] {ECO:0000313|EMBL:EED92353.1, ECO:0000313|Proteomes:UP000001449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1335 {ECO:0000313|EMBL:EED92353.1};
RX PubMed=15459382; DOI=10.1126/science.1101156;
RA Armbrust E.V., Berges J.A., Bowler C., Green B.R., Martinez D.,
RA Putnam N.H., Zhou S., Allen A.E., Apt K.E., Bechner M., Brzezinski M.A.,
RA Chaal B.K., Chiovitti A., Davis A.K., Demarest M.S., Detter J.C.,
RA Glavina T., Goodstein D., Hadi M.Z., Hellsten U., Hildebrand M.,
RA Jenkins B.D., Jurka J., Kapitonov V.V., Kroger N., Lau W.W., Lane T.W.,
RA Larimer F.W., Lippmeier J.C., Lucas S., Medina M., Montsant A., Obornik M.,
RA Parker M.S., Palenik B., Pazour G.J., Richardson P.M., Rynearson T.A.,
RA Saito M.A., Schwartz D.C., Thamatrakoln K., Valentin K., Vardi A.,
RA Wilkerson F.P., Rokhsar D.S.;
RT "The genome of the diatom Thalassiosira pseudonana: ecology, evolution, and
RT metabolism.";
RL Science 306:79-86(2004).
RN [2] {ECO:0000313|EMBL:EED92353.1, ECO:0000313|Proteomes:UP000001449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1335 {ECO:0000313|EMBL:EED92353.1};
RX PubMed=18923393; DOI=10.1038/nature07410;
RA Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A.,
RA Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.,
RA Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P.,
RA Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C.,
RA Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D.,
RA Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G.,
RA La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J.,
RA Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A.,
RA Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L.,
RA Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A.,
RA Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R.,
RA Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S.,
RA Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA Grigoriev I.V.;
RT "The Phaeodactylum genome reveals the evolutionary history of diatom
RT genomes.";
RL Nature 456:239-244(2008).
CC -!- SIMILARITY: Belongs to the FabD family.
CC {ECO:0000256|ARBA:ARBA00008217}.
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DR EMBL; CM000642; EED92353.1; -; Genomic_DNA.
DR RefSeq; XP_002290601.1; XM_002290565.1.
DR AlphaFoldDB; B8C2A9; -.
DR STRING; 35128.B8C2A9; -.
DR PaxDb; 35128-Thaps5219; -.
DR EnsemblProtists; EED92353; EED92353; THAPSDRAFT_5219.
DR GeneID; 7446406; -.
DR KEGG; tps:THAPSDRAFT_5219; -.
DR eggNOG; KOG2926; Eukaryota.
DR HOGENOM; CLU_030558_2_0_1; -.
DR InParanoid; B8C2A9; -.
DR OMA; AANYNCP; -.
DR Proteomes; UP000001449; Chromosome 5.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
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; IPR004410; Malonyl_CoA-ACP_transAc_FabD.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR NCBIfam; TIGR00128; fabD; 1.
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;
KW Acyltransferase {ECO:0000313|EMBL:EED92353.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001449};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:EED92353.1}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..356
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002869629"
FT DOMAIN 57..354
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
SQ SEQUENCE 356 AA; 37511 MW; EDBD8D5C73E377A8 CRC64;
MAPFSSSMIT LFALSALKYS SAFSPASPAF ARRAAASSMR MASDNDFDDF SSKVSFMFPG
QGAQFVGMCG DVCKEVPAAK ALFDEASEIL GYDLLSICTE GPKEKLDSTV VSQPAIFVAS
MAAVEKLRQE EGQDAVDAAT CAMGLSLGEY SALCFAGAIS FADGVKVTKA RGEAMQAASD
AIDTGMVSVI GLDKEKCTEL CEAASEKSGE KIQIANLLCD GNYAVSGHMK ACDVVAEIAK
PDFKARMTVK LAVAGAFHTD FMAPAVDSLK EVLEGIDIQK PRIPVISNVD AKPHSDPATI
KELLAKQVTS PVLWEDSMAS MLEHGFERAV ELGPGKVTTG VLKRINKTAA SSNVEV
//
