FABD_ECOLI
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 03-AUG-2022, entry version 129.
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; Proteobacteria; 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 SWISS-2DPAGE; P0AAI9; -.
DR jPOST; P0AAI9; -.
DR PaxDb; P0AAI9; -.
DR PRIDE; P0AAI9; -.
DR EnsemblBacteria; AAC74176; AAC74176; b1092.
DR EnsemblBacteria; BAA35900; BAA35900; BAA35900.
DR GeneID; 66670642; -.
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 PhylomeDB; P0AAI9; -.
DR BioCyc; EcoCyc:MALONYL-COA-ACP-TRANSACYL-MON; -.
DR BioCyc; MetaCyc:MALONYL-COA-ACP-TRANSACYL-MON; -.
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; 3.40.366.10; -; 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 Pfam; PF00698; Acyl_transf_1; 1.
DR PIRSF; PIRSF000446; Mct; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR TIGRFAMs; TIGR00128; fabD; 1.
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
