ID Q4SA94_TETNG Unreviewed; 372 AA.
AC Q4SA94;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Chromosome 19 SCAF14691, whole genome shotgun sequence {ECO:0000313|EMBL:CAG02438.1};
DE SubName: Full=Malonyl CoA:ACP acyltransferase (mitochondrial) {ECO:0000313|Ensembl:ENSTNIP00000014365.1};
GN ORFNames=GSTENG00021556001 {ECO:0000313|EMBL:CAG02438.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|EMBL:CAG02438.1};
RN [1] {ECO:0000313|EMBL:CAG02438.1, ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|EMBL:CAG02438.1}
RP NUCLEOTIDE SEQUENCE.
RG Genoscope;
RG Whitehead Institute Centre for Genome Research;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSTNIP00000014365.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
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DR EMBL; CAAE01014691; CAG02438.1; -; Genomic_DNA.
DR STRING; 99883.ENSTNIP00000014365; -.
DR Ensembl; ENSTNIT00000014564.1; ENSTNIP00000014365.1; ENSTNIG00000011421.1.
DR KEGG; tng:GSTEN00021556G001; -.
DR GeneTree; ENSGT00390000013715; -.
DR HOGENOM; CLU_030558_2_1_1; -.
DR OMA; AANYNCP; -.
DR TreeFam; TF313401; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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 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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000007303}.
FT DOMAIN 59..370
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
SQ SEQUENCE 372 AA; 41117 MW; 4A5F418D096610FE CRC64;
MLPSVVPRAS RGKVRTLVSL IRRRCSAQPG SSTKDEAAFL TEAKQRRPSA DPSAHSVLLF
PGQGSQFVGM GRGLLKYPNV REMFRVAQKI LGYDLLSLCS EGPPEELMKT VHCQPAVFVT
SLAAVEKLNH ENPKVIESCV AAAGFSVGEF AALVFSGSMN FAEALYAVKV RAEAMQKASE
MVPGGMLSVI GKPQAQYKYA CLQAREYCKS VGIKEPVCSV ANYLFPDARV IAGHKKALDF
LQQNSRQLQF MRVKALPVSG AFHTELMQSA VEPLRDVLRQ VEVRRPEIGV YSNVDGKRYM
SDSHVRKQLG KQLVSPVKWE QTLHEIYERM QGKKFPYTYE VGPGKQLGAT LQKCNRKAFA
NYAHVDATAS QE
//
