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Database: UniProt
Entry: A0A1J5LPQ1_9BACT
LinkDB: A0A1J5LPQ1_9BACT
Original site: A0A1J5LPQ1_9BACT 
ID   A0A1J5LPQ1_9BACT        Unreviewed;       311 AA.
AC   A0A1J5LPQ1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=NAD-dependent epimerase/dehydratase domain-containing protein {ECO:0000259|Pfam:PF01370};
GN   ORFNames=BM564_05245 {ECO:0000313|EMBL:OIQ29617.1};
OS   Bacteroidetes bacterium MedPE-SWsnd-G2.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1860095 {ECO:0000313|EMBL:OIQ29617.1, ECO:0000313|Proteomes:UP000183188};
RN   [1] {ECO:0000313|EMBL:OIQ29617.1, ECO:0000313|Proteomes:UP000183188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MedPE-SWsnd-G2 {ECO:0000313|EMBL:OIQ29617.1};
RX   PubMed=27446036; DOI=10.3389/fmicb.2016.00996;
RA   Lopez-Perez M., Kimes N.E., Haro-Moreno J.M., Rodriguez-Valera F.;
RT   "Not All Particles Are Equal: The Selective Enrichment of Particle-
RT   Associated Bacteria from the Mediterranean Sea.";
RL   Front. Microbiol. 7:996-996(2016).
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. Dihydroflavonol-4-reductase subfamily.
CC       {ECO:0000256|ARBA:ARBA00023445}.
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:OIQ29617.1}.
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DR   EMBL; MPDE01000004; OIQ29617.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J5LPQ1; -.
DR   STRING; 1860095.BM564_05245; -.
DR   Proteomes; UP000183188; 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; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR10366:SF564; 3BETA_HSD DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR10366; NAD DEPENDENT EPIMERASE/DEHYDRATASE; 1.
DR   Pfam; PF01370; Epimerase; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          5..249
FT                   /note="NAD-dependent epimerase/dehydratase"
FT                   /evidence="ECO:0000259|Pfam:PF01370"
SQ   SEQUENCE   311 AA;  34920 MW;  6813D74ED897B76D CRC64;
     MNKVAIIGGS GYIGSYITKL FLQNHYLVKV SVRDLSRKDK FKHLMLLPNT DNLFVSELDI
     MNQLALEDFI DDCDILIHCG TPFQLDVETP SQVETPTVSG TKNFLNCLLH HSTLKKVVVV
     ASVAALNTNF PFPVPNYPES HVYSELDKPY YNEECPPYAR AKFNANVEVT NFLKEHRSLN
     FELTSVSPVF VIGKPLSDRE DSTSVNLLYY FKNNIAGSAF IKLLYETNIN MAVVDVQDVA
     MSIFKTATTL GTHGKNYLLS SESWKVSDIK LMLNKKVTEG GPSIVYSSDL IQKDLGLFFK
     SARTSLHHFS N
//
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