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Database: UniProt
Entry: A0A1Q3TRF5_9SPHI
LinkDB: A0A1Q3TRF5_9SPHI
Original site: A0A1Q3TRF5_9SPHI 
ID   A0A1Q3TRF5_9SPHI        Unreviewed;       319 AA.
AC   A0A1Q3TRF5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=LPS biosynthesis protein WbpP {ECO:0000313|EMBL:OJW05026.1};
GN   ORFNames=BGO52_21325 {ECO:0000313|EMBL:OJW05026.1};
OS   Sphingobacteriales bacterium 44-61.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX   NCBI_TaxID=1895838 {ECO:0000313|EMBL:OJW05026.1, ECO:0000313|Proteomes:UP000186208};
RN   [1] {ECO:0000313|EMBL:OJW05026.1, ECO:0000313|Proteomes:UP000186208}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=44-61 {ECO:0000313|EMBL:OJW05026.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. {ECO:0000256|ARBA:ARBA00007637}.
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:OJW05026.1}.
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DR   EMBL; MKTW01000001; OJW05026.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3TRF5; -.
DR   STRING; 1895838.BGO52_21325; -.
DR   Proteomes; UP000186208; Unassembled WGS sequence.
DR   CDD; cd05256; UDP_AE_SDR_e; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43000:SF7; DTDP-D-GLUCOSE 4,6-DEHYDRATASE; 1.
DR   PANTHER; PTHR43000; DTDP-D-GLUCOSE 4,6-DEHYDRATASE-RELATED; 1.
DR   Pfam; PF01370; Epimerase; 1.
DR   PRINTS; PR01713; NUCEPIMERASE.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
FT   DOMAIN          3..245
FT                   /note="NAD-dependent epimerase/dehydratase"
FT                   /evidence="ECO:0000259|Pfam:PF01370"
SQ   SEQUENCE   319 AA;  34781 MW;  BA44E99339855024 CRC64;
     MRILVTGGCG FIGSNLVEKL LADKRVSFVR ILDNLATGSV ANILPFRDHP SVEFMEGDIR
     DYNTCIAACN SIDRISHQAA LGSVPRSIKD PLTTNNVNIT GTLNVFTAAK ESGIKRIVFA
     ASSSTYGDHP GLPKVEDRIG RPLSPYAVTK YVNELYARVY ADLYGIEFIG LRYFNIFGPK
     QNPNGPYAAV IPLFAESILK GVMPTINGDG SHSRDFTFVD NAVNANILSL FSEEPGALNQ
     IYNIACGEQT SLTQLFEYLA AEAGVTGKPN YGPERTGDVK HSLADISKAK QLLGYEPSVS
     IKQGLKKTFE WFKGNSRSR
//
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