ID   FABD_MYCS2              Reviewed;         290 AA.
AC   A0R0B2; I7GBV9;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Malonyl CoA-acyl carrier protein transacylase;
DE            Short=MCT;
DE            EC=2.3.1.39;
GN   Name=fabD; OrderedLocusNames=MSMEG_4325, MSMEI_4225;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   PUPYLATION AT LYS-157, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20094657; DOI=10.1039/b916104j;
RA   Watrous J., Burns K., Liu W.T., Patel A., Hook V., Bafna V.,
RA   Barry C.E. III, Bark S., Dorrestein P.C.;
RT   "Expansion of the mycobacterial 'PUPylome'.";
RL   Mol. Biosyst. 6:376-385(2010).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AFP40681.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000480; ABK74111.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP40681.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_888600.1; NC_008596.1.
DR   AlphaFoldDB; A0R0B2; -.
DR   SMR; A0R0B2; -.
DR   STRING; 246196.MSMEG_4325; -.
DR   PaxDb; 246196-MSMEI_4225; -.
DR   KEGG; msg:MSMEI_4225; -.
DR   KEGG; msm:MSMEG_4325; -.
DR   PATRIC; fig|246196.19.peg.4243; -.
DR   eggNOG; COG0331; Bacteria.
DR   OrthoDB; 3248271at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
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; 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   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   1: Evidence at protein level;
KW   Acyltransferase; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Isopeptide bond; Lipid biosynthesis; Lipid metabolism; Reference proteome;
KW   Transferase; Ubl conjugation.
FT   CHAIN           1..290
FT                   /note="Malonyl CoA-acyl carrier protein transacylase"
FT                   /id="PRO_0000396808"
FT   ACT_SITE        75
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        178
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        157
FT                   /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT                   with Q-Cter in protein Pup)"
FT                   /evidence="ECO:0000269|PubMed:20094657"
SQ   SEQUENCE   290 AA;  29676 MW;  06BFFF38EEDC5B69 CRC64;
     MLTPWLELPG AADRLAAWSQ ISGLDLTTLG TTATAEEITD TAVTQPLVVA ATLLAHEELT
     KRGHSAAETI VAGHSVGEIA AYAIAGVISA DDAVKLAATR GAEMAKACAV EPTGMAAVLG
     GDEAEVLARL EALDLVPANR NAAGQIVAAG AVAALDKLAE DPPAKARVRK LATAGAFHTH
     YMASALDGYA AAAQSVTTSE PTATLLSNAD GQPVASAADA MEKLVAQLTK PVRWDLCTAT
     LRDRFQNAES AGIVEFPPAG TLVGIAKREL KGTPTRAIKS PEDLDGLDQL
//