MABA_MYCTO
ID MABA_MYCTO Reviewed; 247 AA.
AC P9WGT2; L0T9R6; P0A5Y4; P71764; Q48930;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 40.
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=fabG1;
GN OrderedLocusNames=MT1530;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK45795.1; -; Genomic_DNA.
DR PIR; F70710; F70710.
DR RefSeq; WP_003898892.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WGT2; -.
DR SMR; P9WGT2; -.
DR EnsemblBacteria; AAK45795; AAK45795; MT1530.
DR GeneID; 45425462; -.
DR KEGG; mtc:MT1530; -.
DR PATRIC; fig|83331.31.peg.1645; -.
DR HOGENOM; CLU_010194_1_3_11; -.
DR BioCyc; MetaCyc:G185E-5667-MON; -.
DR UniPathway; UPA00915; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..247
FT /note="3-oxoacyl-[acyl-carrier-protein] reductase MabA"
FT /id="PRO_0000428307"
FT ACT_SITE 153
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 25..27
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P9WGT3"
FT BINDING 47
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P9WGT3"
FT BINDING 61..62
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P9WGT3"
FT BINDING 90
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P9WGT3"
FT BINDING 153
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P71534"
FT BINDING 157
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P71534"
FT BINDING 186
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P71534"
FT BINDING 197
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P71534"
FT SITE 140
FT /note="Important for activity"
FT /evidence="ECO:0000250|UniProtKB:P9WGT3"
SQ SEQUENCE 247 AA; 25697 MW; 70F6254B0FFFCD47 CRC64;
MTATATEGAK PPFVSRSVLV TGGNRGIGLA IAQRLAADGH KVAVTHRGSG APKGLFGVEC
DVTDSDAVDR AFTAVEEHQG PVEVLVSNAG LSADAFLMRM TEEKFEKVIN ANLTGAFRVA
QRASRSMQRN KFGRMIFIGS VSGSWGIGNQ ANYAASKAGV IGMARSIARE LSKANVTANV
VAPGYIDTDM TRALDERIQQ GALQFIPAKR VGTPAEVAGV VSFLASEDAS YISGAVIPVD
GGMGMGH
