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Database: UniProt
Entry: A0A1A2L3N6_9MYCO
LinkDB: A0A1A2L3N6_9MYCO
Original site: A0A1A2L3N6_9MYCO 
ID   A0A1A2L3N6_9MYCO        Unreviewed;       341 AA.
AC   A0A1A2L3N6;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=2-dehydropantoate 2-reductase {ECO:0000313|EMBL:OBG84770.1};
GN   ORFNames=A5699_25905 {ECO:0000313|EMBL:OBG84770.1};
OS   Mycobacterium sp. E802.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1834152 {ECO:0000313|EMBL:OBG84770.1, ECO:0000313|Proteomes:UP000092062};
RN   [1] {ECO:0000313|EMBL:OBG84770.1, ECO:0000313|Proteomes:UP000092062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E802 {ECO:0000313|EMBL:OBG84770.1,
RC   ECO:0000313|Proteomes:UP000092062};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OBG84770.1}.
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DR   EMBL; LZJD01000094; OBG84770.1; -; Genomic_DNA.
DR   RefSeq; WP_067770380.1; NZ_LZJD01000094.1.
DR   AlphaFoldDB; A0A1A2L3N6; -.
DR   Proteomes; UP000092062; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR   PANTHER; PTHR43765:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR   Pfam; PF02558; ApbA; 1.
DR   Pfam; PF08546; ApbA_C; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
FT   DOMAIN          10..146
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          187..301
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   341 AA;  36363 MW;  09678DD42B7B24D8 CRC64;
     MARTLTRPFV VYGVGAIGGV IAGQLRLAGY DVTAVARGAH LNAIRTCGLT LVTQAGTDVV
     DLPAAADAGE VDWSTRPVVI LAVKSHQTAA ALDDLSAHAP ADTPVFVAQN GVANEAAALR
     RFANVYGVTV MLPAAHLDPG VVIQQSHPVA GILDLGRYPT GRDALAEQIC SALRVARFES
     QVRDDVMAWK YRKLIANLGN GVIAAYRPGP QADTLIARAR EEAERVLTAA GISFVTAEQD
     AQRRGDLLQG RVHDDYFSST WQSVARGHTQ VETDWFNGEI VLQARLHGQS APVNELIQRV
     TAEHARVGRP VRSLDAAAAL KKLGPEPDAQ FRHDIVVTTS A
//
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