MABA_MYCS2
ID MABA_MYCS2 Reviewed; 255 AA.
AC P71534; A0QX27; I7FLD4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase MabA {ECO:0000305};
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=Acetoacetyl-CoA reductase {ECO:0000305};
DE EC=1.1.1.36 {ECO:0000269|PubMed:29717709};
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:0000303|PubMed:29717709}; Synonyms=fabG;
GN OrderedLocusNames=MSMEG_3150, MSMEI_3069;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Banerjee A., Sugantino M., Sacchettini J.C., Jacobs W.R. Jr.;
RT "Molecular cloning, expression and characterization of 3-ketoacyl reductase
RT from mycobacteria.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
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 [5] {ECO:0007744|PDB:5OVJ, ECO:0007744|PDB:5OVK, ECO:0007744|PDB:5OVL}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH
RP NADP AND NADPH, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND DOMAIN.
RX PubMed=29717709; DOI=10.1107/s2059798318002917;
RA Kussau T., Flipo M., Van Wyk N., Viljoen A., Olieric V., Kremer L.,
RA Blaise M.;
RT "Structural rearrangements occurring upon cofactor binding in the
RT Mycobacterium smegmatis beta-ketoacyl-acyl carrier protein reductase
RT MabA.";
RL Acta Crystallogr. D 74:383-393(2018).
CC -!- FUNCTION: Part of the mycobacterial fatty acid elongation system FAS-
CC II, which is involved in mycolic acid biosynthesis (By similarity).
CC Catalyzes the NADPH-dependent reduction of beta-ketoacyl derivatives,
CC the second step of the FAS-II elongation cycle (By similarity). Has a
CC preference for longer substrates (PubMed:29717709). Can use CoA
CC derivatives as substrates in vitro (PubMed:29717709).
CC {ECO:0000250|UniProtKB:P9WGT3, ECO:0000269|PubMed:29717709}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-3-hydroxyacyl-CoA + NADP(+) = a 3-oxoacyl-CoA + H(+) +
CC NADPH; Xref=Rhea:RHEA:22256, ChEBI:CHEBI:15378, ChEBI:CHEBI:57319,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:90726; EC=1.1.1.36;
CC Evidence={ECO:0000269|PubMed:29717709};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22258;
CC Evidence={ECO:0000269|PubMed:29717709};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-3-hydroxybutanoyl-CoA + NADP(+) = acetoacetyl-CoA + H(+)
CC + NADPH; Xref=Rhea:RHEA:45796, ChEBI:CHEBI:15378, ChEBI:CHEBI:57286,
CC ChEBI:CHEBI:57315, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:29717709};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45798;
CC Evidence={ECO:0000269|PubMed:29717709};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyoctanoyl-CoA + NADP(+) = 3-oxooctanoyl-CoA + H(+)
CC + NADPH; Xref=Rhea:RHEA:45844, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:62619, ChEBI:CHEBI:74279;
CC Evidence={ECO:0000269|PubMed:29717709};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45846;
CC Evidence={ECO:0000269|PubMed:29717709};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.5 mM for acetoacetyl-CoA {ECO:0000269|PubMed:29717709};
CC KM=0.6 mM for beta-keto-octanoyl-CoA {ECO:0000269|PubMed:29717709};
CC Note=kcat is 1.14 sec(-1) with acetoacetyl-CoA as substrate. kcat is
CC 5.72 sec(-1) with beta-keto-octanoyl-CoA as substrate.
CC {ECO:0000269|PubMed:29717709};
CC -!- PATHWAY: Lipid metabolism; mycolic acid biosynthesis.
CC {ECO:0000250|UniProtKB:P9WGT3}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:29717709}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000250|UniProtKB:P9WGT3}.
CC -!- DOMAIN: Upon NADPH binding, several residues are pushed away from the
CC active site, allowing the enzyme to adopt an open conformation. The
CC transition from an NADPH-bound to an NADP(+)-bound form is likely to
CC facilitate release of the product. {ECO:0000269|PubMed:29717709}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AFP39533.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U66800; AAC69638.1; -; Genomic_DNA.
DR EMBL; CP000480; ABK71816.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP39533.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011728850.1; NZ_SIJM01000002.1.
DR RefSeq; YP_887465.1; NC_008596.1.
DR PDB; 5OVJ; X-ray; 1.70 A; A/B=1-255.
DR PDB; 5OVK; X-ray; 1.45 A; A/B/C/D=1-255.
DR PDB; 5OVL; X-ray; 2.40 A; A/B/C/D=1-255.
DR PDBsum; 5OVJ; -.
DR PDBsum; 5OVK; -.
DR PDBsum; 5OVL; -.
DR AlphaFoldDB; P71534; -.
DR SMR; P71534; -.
DR STRING; 246196.MSMEI_3069; -.
DR EnsemblBacteria; ABK71816; ABK71816; MSMEG_3150.
DR EnsemblBacteria; AFP39533; AFP39533; MSMEI_3069.
DR GeneID; 66734551; -.
DR KEGG; msg:MSMEI_3069; -.
DR KEGG; msm:MSMEG_3150; -.
DR PATRIC; fig|246196.19.peg.3111; -.
DR eggNOG; COG1028; Bacteria.
DR OMA; KMPERDY; -.
DR OrthoDB; 1601931at2; -.
DR UniPathway; UPA00915; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
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:0018454; F:acetoacetyl-CoA reductase activity; IEA:UniProtKB-EC.
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 1: Evidence at protein level;
KW 3D-structure; Cell wall; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase;
KW Reference proteome; Secreted.
FT CHAIN 1..255
FT /note="3-oxoacyl-[acyl-carrier-protein] reductase MabA"
FT /id="PRO_0000054674"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 32..35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:29717709"
FT BINDING 55
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:29717709"
FT BINDING 69..70
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:29717709"
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:0000269|PubMed:29717709"
FT BINDING 165
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:29717709"
FT BINDING 194
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:29717709"
FT BINDING 205
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:29717709"
FT SITE 148
FT /note="Important for activity"
FT /evidence="ECO:0000250|UniProtKB:P9WGT3"
FT CONFLICT 75
FT /note="A -> G (in Ref. 1; AAC69638)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="A -> D (in Ref. 1; AAC69638)"
FT /evidence="ECO:0000305"
FT CONFLICT 189..190
FT /note="VA -> LP (in Ref. 1; AAC69638)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="A -> G (in Ref. 1; AAC69638)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="L -> I (in Ref. 1; AAC69638)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="A -> D (in Ref. 1; AAC69638)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="A -> V (in Ref. 1; AAC69638)"
FT /evidence="ECO:0000305"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:5OVK"
FT HELIX 34..46
FT /evidence="ECO:0007829|PDB:5OVK"
FT STRAND 49..57
FT /evidence="ECO:0007829|PDB:5OVK"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:5OVK"
FT HELIX 73..87
FT /evidence="ECO:0007829|PDB:5OVK"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:5OVK"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:5OVK"
FT HELIX 110..120
FT /evidence="ECO:0007829|PDB:5OVK"
FT HELIX 122..138
FT /evidence="ECO:0007829|PDB:5OVK"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:5OVK"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:5OVK"
FT HELIX 159..179
FT /evidence="ECO:0007829|PDB:5OVK"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:5OVK"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:5OVK"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:5OVL"
FT HELIX 197..201
FT /evidence="ECO:0007829|PDB:5OVK"
FT HELIX 204..211
FT /evidence="ECO:0007829|PDB:5OVK"
FT HELIX 222..233
FT /evidence="ECO:0007829|PDB:5OVK"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:5OVL"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:5OVK"
FT TURN 249..252
FT /evidence="ECO:0007829|PDB:5OVK"
SQ SEQUENCE 255 AA; 26641 MW; BAE0131C09C472DB CRC64;
MTVTDNPADT AGEATAGRPA FVSRSVLVTG GNRGIGLAIA RRLAADGHKV AVTHRGSGAP
DDLFGVQCDV TDSAAVDRAF KEVEEHQGPV EVLVANAGIS KDAFLMRMTE ERFEEVINTN
LTGAFRCAQR ASRTMQRKRF GRIIFIGSVS GMWGIGNQAN YAAAKAGLIG MARSISRELA
KAGVTANVVA PGYIDTEMTR ALDERIQAGA LDFIPAKRVG TAEEVAGAVS FLASEDASYI
AGAVIPVDGG MGMGH
