ID   FABD_ECOLI              Reviewed;         309 AA.
AC   P0AAI9; P25715;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   24-JAN-2024, entry version 136.
DE   RecName: Full=Malonyl CoA-acyl carrier protein transacylase;
DE            Short=MCT;
DE            EC=2.3.1.39;
GN   Name=fabD; Synonyms=tfpA; OrderedLocusNames=b1092, JW1078;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11.
RC   STRAIN=K12;
RX   PubMed=1339356; DOI=10.1016/0014-5793(92)80128-4;
RA   Magnuson K., Oh W., Larson T.J., Cronan J.E. Jr.;
RT   "Cloning and nucleotide sequence of the fabD gene encoding malonyl coenzyme
RT   A-acyl carrier protein transacylase of Escherichia coli.";
RL   FEBS Lett. 299:262-266(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1314802; DOI=10.1128/jb.174.9.2851-2857.1992;
RA   Verwoert I.I.G.S., Verbree E.C., van der Linden K.H., Nijkamp H.J.,
RA   Stuitje A.R.;
RT   "Cloning, nucleotide sequence, and expression of the Escherichia coli fabD
RT   gene, encoding malonyl coenzyme A-acyl carrier protein transacylase.";
RL   J. Bacteriol. 174:2851-2857(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7700236; DOI=10.1007/bf00298970;
RA   Bouquin N., Tempete M., Holland I.B., Seror S.J.;
RT   "Resistance to trifluoroperazine, a calmodulin inhibitor, maps to the fabD
RT   locus in Escherichia coli.";
RL   Mol. Gen. Genet. 246:628-637(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 289-309.
RC   STRAIN=K12;
RX   PubMed=1556094; DOI=10.1016/s0021-9258(18)42616-6;
RA   Rawlings M., Cronan J.E. Jr.;
RT   "The gene encoding Escherichia coli acyl carrier protein lies within a
RT   cluster of fatty acid biosynthetic genes.";
RL   J. Biol. Chem. 267:5751-5754(1992).
RN   [8]
RP   PROTEIN SEQUENCE OF 2-12.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA   Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S.,
RA   Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.;
RL   Submitted (SEP-1994) to UniProtKB.
RN   [9]
RP   PROTEIN SEQUENCE OF 2-11.
RC   STRAIN=K12 / EMG2;
RX   PubMed=9298646; DOI=10.1002/elps.1150180807;
RA   Link A.J., Robison K., Church G.M.;
RT   "Comparing the predicted and observed properties of proteins encoded in the
RT   genome of Escherichia coli K-12.";
RL   Electrophoresis 18:1259-1313(1997).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX   PubMed=7768883; DOI=10.1074/jbc.270.22.12961;
RA   Serre L., Verbree E.C., Dauter Z., Stuitje A.R., Derewenda Z.S.;
RT   "The Escherichia coli malonyl-CoA:acyl carrier protein transacylase at 1.5-
RT   A resolution. Crystal structure of a fatty acid synthase component.";
RL   J. Biol. Chem. 270:12961-12964(1995).
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   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SIMILARITY: Belongs to the FabD family. {ECO:0000305}.
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DR   EMBL; M87040; AAA23742.1; -; Genomic_DNA.
DR   EMBL; Z11565; CAA77658.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74176.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35900.1; -; Genomic_DNA.
DR   EMBL; M84991; AAA23738.1; -; Genomic_DNA.
DR   PIR; B41856; B41856.
DR   RefSeq; NP_415610.1; NC_000913.3.
DR   RefSeq; WP_000191372.1; NZ_STEB01000016.1.
DR   PDB; 1MLA; X-ray; 1.50 A; A=1-309.
DR   PDB; 2G1H; X-ray; 1.86 A; A=2-309.
DR   PDB; 2G2O; X-ray; 1.76 A; A=2-309.
DR   PDB; 2G2Y; X-ray; 2.26 A; A=2-309.
DR   PDB; 2G2Z; X-ray; 2.80 A; A=2-309.
DR   PDB; 6U0J; X-ray; 1.90 A; A=1-309.
DR   PDBsum; 1MLA; -.
DR   PDBsum; 2G1H; -.
DR   PDBsum; 2G2O; -.
DR   PDBsum; 2G2Y; -.
DR   PDBsum; 2G2Z; -.
DR   PDBsum; 6U0J; -.
DR   AlphaFoldDB; P0AAI9; -.
DR   SMR; P0AAI9; -.
DR   BioGRID; 4263368; 375.
DR   DIP; DIP-47923N; -.
DR   IntAct; P0AAI9; 4.
DR   STRING; 511145.b1092; -.
DR   SwissLipids; SLP:000001778; -.
DR   jPOST; P0AAI9; -.
DR   PaxDb; 511145-b1092; -.
DR   EnsemblBacteria; AAC74176; AAC74176; b1092.
DR   GeneID; 75203678; -.
DR   GeneID; 945766; -.
DR   KEGG; ecj:JW1078; -.
DR   KEGG; eco:b1092; -.
DR   PATRIC; fig|1411691.4.peg.1176; -.
DR   EchoBASE; EB1293; -.
DR   eggNOG; COG0331; Bacteria.
DR   HOGENOM; CLU_030558_0_0_6; -.
DR   InParanoid; P0AAI9; -.
DR   OMA; AANYNCP; -.
DR   OrthoDB; 9808564at2; -.
DR   PhylomeDB; P0AAI9; -.
DR   BioCyc; EcoCyc:MALONYL-COA-ACP-TRANSACYL-MONOMER; -.
DR   BioCyc; MetaCyc:MALONYL-COA-ACP-TRANSACYL-MONOMER; -.
DR   BRENDA; 2.3.1.39; 2026.
DR   UniPathway; UPA00094; -.
DR   EvolutionaryTrace; P0AAI9; -.
DR   PRO; PR:P0AAI9; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IDA:EcoCyc.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IMP:EcoCyc.
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; PTHR42681; MALONYL-COA-ACYL CARRIER PROTEIN TRANSACYLASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42681:SF1; MALONYL-COA-ACYL CARRIER PROTEIN TRANSACYLASE, MITOCHONDRIAL; 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.
DR   SWISS-2DPAGE; P0AAI9; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Direct protein sequencing;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1339356,
FT                   ECO:0000269|PubMed:9298646, ECO:0000269|Ref.8"
FT   CHAIN           2..309
FT                   /note="Malonyl CoA-acyl carrier protein transacylase"
FT                   /id="PRO_0000194213"
FT   ACT_SITE        92
FT   ACT_SITE        201
FT   STRAND          4..8
FT                   /evidence="ECO:0007829|PDB:1MLA"
FT   TURN            16..19
FT                   /evidence="ECO:0007829|PDB:1MLA"
FT   HELIX           20..25
FT                   /evidence="ECO:0007829|PDB:1MLA"
FT   HELIX           28..40
FT                   /evidence="ECO:0007829|PDB:1MLA"
FT   HELIX           44..50
FT                   /evidence="ECO:0007829|PDB:1MLA"
FT   HELIX           53..56
FT                   /evidence="ECO:0007829|PDB:1MLA"
FT   HELIX           59..79
FT                   /evidence="ECO:0007829|PDB:1MLA"
FT   STRAND          86..91
FT                   /evidence="ECO:0007829|PDB:1MLA"
FT   HELIX           93..101
FT                   /evidence="ECO:0007829|PDB:1MLA"
FT   HELIX           107..124
FT                   /evidence="ECO:0007829|PDB:1MLA"
FT   STRAND          129..137
FT                   /evidence="ECO:0007829|PDB:1MLA"
FT   HELIX           140..150
FT                   /evidence="ECO:0007829|PDB:1MLA"
FT   STRAND          156..163
FT                   /evidence="ECO:0007829|PDB:1MLA"
FT   STRAND          166..172
FT                   /evidence="ECO:0007829|PDB:1MLA"
FT   HELIX           173..185
FT                   /evidence="ECO:0007829|PDB:1MLA"
FT   STRAND          189..193
FT                   /evidence="ECO:0007829|PDB:1MLA"
FT   HELIX           203..205
FT                   /evidence="ECO:0007829|PDB:1MLA"
FT   HELIX           206..217
FT                   /evidence="ECO:0007829|PDB:1MLA"
FT   TURN            231..233
FT                   /evidence="ECO:0007829|PDB:1MLA"
FT   HELIX           240..252
FT                   /evidence="ECO:0007829|PDB:1MLA"
FT   HELIX           257..266
FT                   /evidence="ECO:0007829|PDB:1MLA"
FT   STRAND          271..274
FT                   /evidence="ECO:0007829|PDB:1MLA"
FT   STRAND          276..279
FT                   /evidence="ECO:0007829|PDB:1MLA"
FT   HELIX           280..288
FT                   /evidence="ECO:0007829|PDB:1MLA"
FT   STRAND          293..296
FT                   /evidence="ECO:0007829|PDB:1MLA"
FT   HELIX           300..306
FT                   /evidence="ECO:0007829|PDB:1MLA"
SQ   SEQUENCE   309 AA;  32417 MW;  3572E0681D14AB4A CRC64;
     MTQFAFVFPG QGSQTVGMLA DMAASYPIVE ETFAEASAAL GYDLWALTQQ GPAEELNKTW
     QTQPALLTAS VALYRVWQQQ GGKAPAMMAG HSLGEYSALV CAGVIDFADA VRLVEMRGKF
     MQEAVPEGTG AMAAIIGLDD ASIAKACEEA AEGQVVSPVN FNSPGQVVIA GHKEAVERAG
     AACKAAGAKR ALPLPVSVPS HCALMKPAAD KLAVELAKIT FNAPTVPVVN NVDVKCETNG
     DAIRDALVRQ LYNPVQWTKS VEYMAAQGVE HLYEVGPGKV LTGLTKRIVD TLTASALNEP
     SAMAAALEL
//