ID   D2WHE1_RHORH            Unreviewed;       259 AA.
AC   D2WHE1;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase MabA {ECO:0000256|ARBA:ARBA00040781};
DE   AltName: Full=3-ketoacyl-acyl carrier protein reductase {ECO:0000256|ARBA:ARBA00033040};
DE   AltName: Full=Beta-Ketoacyl-acyl carrier protein reductase {ECO:0000256|ARBA:ARBA00029743, ECO:0000256|ARBA:ARBA00032683};
OS   Rhodococcus rhodochrous.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1829 {ECO:0000313|EMBL:ADB12481.1};
RN   [1] {ECO:0000313|EMBL:ADB12481.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BCRC 10305 {ECO:0000313|EMBL:ADB12481.1};
RA   Lin W.-D., Chen C.-Y., Hsu W.-H.;
RT   "Amino Alcohol Dehydrogenase Gene from Rhodococcus rhodochrous BCRC
RT   10305.";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00023333};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17399;
CC         Evidence={ECO:0000256|ARBA:ARBA00023333};
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000256|ARBA:ARBA00004191}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484}.
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; GQ266679; ADB12481.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2WHE1; -.
DR   CDD; cd05233; SDR_c; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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.
PE   3: Inferred from homology;
KW   Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW   Secreted {ECO:0000256|ARBA:ARBA00022512}.
SQ   SEQUENCE   259 AA;  26581 MW;  B0FE6DDBB5336D9B CRC64;
     MFNSIEGRSV VVTGGSKGIG LGMVRVFARA GANVLMTARD ALTLERAAEG LNGLPGAVST
     LQVDVTNPDS LAGMAEVAAE RHGGIDVLCA NAGIFPSKRL GEMTSEDMDS VFGVNVKGTI
     HAVQACMPWL ETSGRGRVVV TSSITGPVTG YPGWSHYGAS KAAQMGFIRT AAIELAPKRI
     TINAVLPGNV ITEGLDGLGQ EYLDQMASSV PAGSLGSVED IANAALFFAL DEAAYITGQS
     LIVDGGQVLP ESAMALGEL
//