ID   MABA_MYCAV              Reviewed;         255 AA.
AC   O07399;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase MabA {ECO:0000250|UniProtKB:P9WGT3};
DE            EC=1.1.1.100 {ECO:0000250|UniProtKB:P9WGT3};
DE   AltName: Full=3-ketoacyl-acyl carrier protein reductase {ECO:0000250|UniProtKB:P9WGT3};
DE   AltName: Full=Beta-ketoacyl-ACP reductase {ECO:0000250|UniProtKB:P9WGT3};
DE   AltName: Full=Beta-ketoacyl-acyl carrier protein reductase {ECO:0000250|UniProtKB:P9WGT3};
GN   Name=mabA {ECO:0000250|UniProtKB:P9WGT3}; Synonyms=fabG;
OS   Mycobacterium avium.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=1764;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=GIR10;
RX   PubMed=9534249; DOI=10.1099/00221287-144-3-807;
RA   Labo M., Gusberti L., de Rossi E., Speziale P., Riccardi G.;
RT   "Determination of a 15437 bp nucleotide sequence around the inhA gene of
RT   Mycobacterium avium and similarity analysis of the products of putative
RT   ORFs.";
RL   Microbiology 144:807-814(1998).
CC   -!- FUNCTION: Part of the mycobacterial fatty acid elongation system FAS-
CC       II, which is involved in mycolic acid biosynthesis. Catalyzes the
CC       NADPH-dependent reduction of beta-ketoacyl derivatives, the second step
CC       of the FAS-II elongation cycle. {ECO:0000250|UniProtKB:P9WGT3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+)
CC         + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC         COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
CC         Evidence={ECO:0000250|UniProtKB:P9WGT3};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17399;
CC         Evidence={ECO:0000250|UniProtKB:P9WGT3};
CC   -!- PATHWAY: Lipid metabolism; mycolic acid biosynthesis.
CC       {ECO:0000250|UniProtKB:P9WGT3}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P9WGT3}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000250|UniProtKB:P9WGT3}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF002133; AAC46203.1; -; Genomic_DNA.
DR   AlphaFoldDB; O07399; -.
DR   SMR; O07399; -.
DR   UniPathway; UPA00915; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; ISS:UniProtKB.
DR   GO; GO:0050661; F:NADP binding; ISS:UniProtKB.
DR   GO; GO:0030497; P:fatty acid elongation; ISS:UniProtKB.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR42879; 3-OXOACYL-(ACYL-CARRIER-PROTEIN) REDUCTASE; 1.
DR   PANTHER; PTHR42879:SF2; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] REDUCTASE FABG; 1.
DR   Pfam; PF13561; adh_short_C2; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SMART; SM00822; PKS_KR; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Cell wall; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase; Secreted.
FT   CHAIN           1..255
FT                   /note="3-oxoacyl-[acyl-carrier-protein] reductase MabA"
FT                   /id="PRO_0000054675"
FT   ACT_SITE        161
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         33..35
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT3"
FT   BINDING         55
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT3"
FT   BINDING         69..70
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT3"
FT   BINDING         98
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT3"
FT   BINDING         161
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P71534"
FT   BINDING         165
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P71534"
FT   BINDING         194
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P71534"
FT   BINDING         205
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P71534"
FT   SITE            148
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT3"
SQ   SEQUENCE   255 AA;  26706 MW;  C3A20AA0B6251655 CRC64;
     MTDTATENTT ESAADYGRPA FVSRSVLVTG GNRGIGLAIA QRLAAEAHKV AVTHRGSGAP
     DGLFGVECDV TDNDAVDRAF TEVEEHQGPV EVLVSNAGIS KDAFLIRMTE ERFTEVINAN
     LTGAFRVTQR AARSMQKKRF GRIIYIGSVS GMWGIGNQAN YAAAKAGLIG MARSISRELS
     KAGVTANVVA PGYIDTEMTR ALDERIQAGA LEFIPAKRVG TAAEVPGAVS FLASEDASYI
     AGAVIPVDGG MGMGH
//