MABA_MYCAV
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 03-AUG-2022, entry version 98.
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; Actinobacteria; Corynebacteriales; 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}.
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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 InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 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
