ID A4T648_MYCGI Unreviewed; 256 AA.
AC A4T648;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
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};
GN OrderedLocusNames=Mflv_1263 {ECO:0000313|EMBL:ABP43745.1};
OS Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS PYR-GCK)).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350054 {ECO:0000313|EMBL:ABP43745.1};
RN [1] {ECO:0000313|EMBL:ABP43745.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP43745.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABP43745.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP43745.1};
RX PubMed=23469141;
RA Badejo A.C., Badejo A.O., Shin K.H., Chai Y.G.;
RT "A Gene Expression Study of the Activities of Aromatic Ring-Cleavage
RT Dioxygenases in Mycobacterium gilvum PYR-GCK to Changes in Salinity and pH
RT during Pyrene Degradation.";
RL PLoS ONE 8:E58066-E58066(2013).
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, ECO:0000256|RuleBase:RU000363}.
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DR EMBL; CP000656; ABP43745.1; -; Genomic_DNA.
DR AlphaFoldDB; A4T648; -.
DR STRING; 350054.Mflv_1263; -.
DR KEGG; mgi:Mflv_1263; -.
DR eggNOG; COG1028; Bacteria.
DR HOGENOM; CLU_010194_1_1_11; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; 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; PF00106; adh_short; 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 {ECO:0000256|ARBA:ARBA00022512};
KW Secreted {ECO:0000256|ARBA:ARBA00022512}.
SQ SEQUENCE 256 AA; 26379 MW; B7884DC80B11DD0F CRC64;
MSDRFSMEGR VAVITGGGTG IGRASALVLA EHGADVVLAG RRAEPLKETA AEVEALGRRA
LAVPTDVTDA DACQALVDTT LAEFGRLDVL LNNAGGGETK SLMKWTDDEW HHVLDLNLSS
AWYLSRAAAK PMIAQGSGAI VNISSGAGLL AMPQAPIYGA AKAGLQNLTG SMAAAWTRKG
VRVNCIACGA VRTPGLEADA KRQGFDIDMI GQTNGSGRIA EPDEIGYGVL FFASDASSYC
SGQTLYMHGG PGPAGV
//
