ID W2ZKD6_PHYPR Unreviewed; 1453 AA.
AC W2ZKD6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Malonyl-CoA:ACP transacylase (MAT) domain-containing protein {ECO:0000259|SMART:SM00827};
DE Flags: Fragment;
GN ORFNames=F442_06376 {ECO:0000313|EMBL:ETP47733.1};
OS Phytophthora parasitica P10297.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317064 {ECO:0000313|EMBL:ETP47733.1, ECO:0000313|Proteomes:UP000018948};
RN [1] {ECO:0000313|EMBL:ETP47733.1, ECO:0000313|Proteomes:UP000018948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P10297 {ECO:0000313|EMBL:ETP47733.1,
RC ECO:0000313|Proteomes:UP000018948};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P10297.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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:ETP47733.1}.
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DR EMBL; ANIY01001350; ETP47733.1; -; Genomic_DNA.
DR EnsemblProtists; ETP47733; ETP47733; F442_06376.
DR Proteomes; UP000018948; Unassembled WGS sequence.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro.
DR GO; GO:0004317; F:(3R)-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:InterPro.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:InterPro.
DR GO; GO:0004312; F:fatty acid synthase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR Gene3D; 1.20.930.70; -; 1.
DR Gene3D; 3.30.1120.100; -; 1.
DR Gene3D; 3.30.70.3330; -; 1.
DR Gene3D; 3.90.25.70; -; 1.
DR Gene3D; 6.10.140.1400; -; 1.
DR Gene3D; 6.10.60.10; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 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; IPR013785; Aldolase_TIM.
DR InterPro; IPR013565; Fas1/AflB-like_central.
DR InterPro; IPR040883; FAS_meander.
DR InterPro; IPR003965; Fatty_acid_synthase.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR002539; MaoC-like_dom.
DR PANTHER; PTHR10982:SF21; FATTY ACID SYNTHASE SUBUNIT BETA; 1.
DR PANTHER; PTHR10982; MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08354; Fas1-AflB-like_hel; 1.
DR Pfam; PF17951; FAS_meander; 1.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR PRINTS; PR01483; FASYNTHASE.
DR SMART; SM00827; PKS_AT; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000018948}.
FT DOMAIN 962..1418
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT NON_TER 1453
FT /evidence="ECO:0000313|EMBL:ETP47733.1"
SQ SEQUENCE 1453 AA; 159852 MW; 4A44E07D7BD1A92B CRC64;
MPSMTVMLQW TGGRAGGHHS FEDFHQPMEE TYAAIRRVSN VLLVVGSGFG NWEDSKQYLT
GEWSLARGHL FKMPADGILM GSRVMVAKEA ATAPEVKKLL VDTPGIESEL EWETSYTGAI
GGVITVTSEL GEPIHVVANR CTLLWKEFDD KYFSIPRDQV ELALRLNKKD IITRLNADYQ
KPYFGCKRNV ETGESVPADL EEMSYGDVLT RMIDLMYVEV EGKPHRWVHD TFFSRVSKFI
TRTEERFRRE SSGDLFDQSE LKTNPRGTVT AFIAKYPQTV STLLSVPDCD FFLDLCRTGG
KPVNFVPAID TEFKTWFKKD SLWYSEDLDA VPDGDAQRVF ILQGPVAVRY STVVDEPVAD
ILNGIAAGFT NVVKESGAVA AATAVSVKET MDIANVEVTE TDDSVELSIS ADESAVPSAD
EWLASLAASV DDKEWLSALI SSTHVVEEKK WLANPVRQLL VPQVGQKYVV DAAGIRVFDS
SIDISGPVIE ITKKDASISV VVNEVRPAVT GLTAGVVALE MAFQYHPELS CSIHTEGSGF
IDKVKAFYAR FWVAIEGQEE ESCKAACEES VMSPFTAEFS ISKKDIVDYR AALGLSDDEE
GAPADFSTIV SWRPLIQSVF TKEVKGNLLD LVHLKHSYKL LSSRKVSATF LPGDDIVSTS
NVGSLRIIDS GKIVHGVAII SRKTVDSEMV EVLEPLVELH SEFLIRGAFN DFESTFSIDK
STDAFVPKRQ EDVEILKTKS WLKLAAEASV NVGDHLSFEL TTKKQYASIG SLSSVEVTGT
LFREEAGSNV ELGTVEFKSN DANESPVVAF LRQVQPEDAK ASGMFSNGGS HMLEKPLEIN
VPTNALAYAV ASRDLNPIHR SKYAAILGHL PKGKPIMHGL WTATKVRDLV TQNFGLGFDS
NVVDYDVNFD GMVYPGDKLF MQARHIGLDN GKKVLSVEVV NGSGERVVSA RAVVKQAPMA
FVFTGQGSAA VGMGMDRYQE SSVARDIWNR GDTHLRKTFG FSILEMVRKN PKSITVHFGG
KKGLKIRDNY MKLTCEDPVT GKITALLPEI DEDTESFSFS ASEGLLFATQ FSQPALVLLE
KAMFSEIEAA QLIPDDAYFA GHSLGEYAGL ISFAGALTVE ALMDLVFLRG MIMQKSVKRN
AEGRSDYGMV ATNPTRVGPH FTEEAMHKIV DGIEAASGKL LQVVNFNIQQ RQYVVAGENV
NLETLSLALS AVKTLKSTAA EDVQKVIADS LAQARARKEK CEQTGRPFTL ARGLATIPLV
GIDVPFHSRE LLGGVPSFRA LLRTKFDPQV LERQLPLLVN RYIPNLVATP FSLKRSYFEE
VYAATKSPYL EEVLDPMQWK LTSKAQLAHL LVVELLAYQF ASPVQWIKTQ ALLFSEGGVR
RFVEIGPAPT LTNMALRTLQ VGDFPDVSRE ILWYQRDREV VHFEEETSNI SASEYARGLA
AEAAAEAAAT AAK
//
