ID V5WF39_9SPIO Unreviewed; 352 AA.
AC V5WF39;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Dihydroflavonol-4-reductase {ECO:0000313|EMBL:AHC14417.1};
DE EC=1.1.1.219 {ECO:0000313|EMBL:AHC14417.1};
GN ORFNames=L21SP2_0999 {ECO:0000313|EMBL:AHC14417.1};
OS Salinispira pacifica.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Salinispira.
OX NCBI_TaxID=1307761 {ECO:0000313|EMBL:AHC14417.1, ECO:0000313|Proteomes:UP000018680};
RN [1] {ECO:0000313|EMBL:AHC14417.1, ECO:0000313|Proteomes:UP000018680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L21-RPul-D2 {ECO:0000313|EMBL:AHC14417.1,
RC ECO:0000313|Proteomes:UP000018680};
RX PubMed=26203324; DOI=10.1186/1944-3277-10-7;
RA Ben Hania W., Joseph M., Schumann P., Bunk B., Fiebig A., Sproer C.,
RA Klenk H.P., Fardeau M.L., Spring S.;
RT "Complete genome sequence and description of Salinispira pacifica gen.
RT nov., sp. nov., a novel spirochaete isolated form a hypersaline microbial
RT mat.";
RL Stand. Genomic Sci. 10:7-7(2015).
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Dihydroflavonol-4-reductase subfamily.
CC {ECO:0000256|ARBA:ARBA00023445}.
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DR EMBL; CP006939; AHC14417.1; -; Genomic_DNA.
DR RefSeq; WP_024267347.1; NC_023035.1.
DR AlphaFoldDB; V5WF39; -.
DR STRING; 1307761.L21SP2_0999; -.
DR KEGG; slr:L21SP2_0999; -.
DR PATRIC; fig|1307761.3.peg.997; -.
DR eggNOG; COG0451; Bacteria.
DR HOGENOM; CLU_007383_9_2_12; -.
DR OrthoDB; 9778052at2; -.
DR Proteomes; UP000018680; Chromosome.
DR GO; GO:0045552; F:dihydrokaempferol 4-reductase activity; IEA:UniProtKB-EC.
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,
KW ECO:0000313|EMBL:AHC14417.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018680}.
FT DOMAIN 10..254
FT /note="NAD-dependent epimerase/dehydratase"
FT /evidence="ECO:0000259|Pfam:PF01370"
SQ SEQUENCE 352 AA; 38845 MW; FB17ABFB063FA535 CRC64;
MENAENFSPV AVTGGSGYIA SWIVLKLLER GIEVHTTVRN LSDERKVGHL KTMQKNFPGQ
LSLFEADLNI EGSFDAAIAD CEALIHSASP FVISNISDPE LELIRPAKVG TENVLRSADR
AQTVRKVVLT SSVAAVHTDN NEWKNTSEGI LNENHWNSTA SAKYQPYSYS KTLAEKAAWE
YAQQQDHWEL AVINPSFVVG PSLSKRLDGT SSSTVAGFFT GQFKQGIPDL HFGMVDVRDV
AQAHILALEN PEAKGRFILM SEEMSLPEAG RILQNMQNGK LPVNLRVLPK ALFYVMGPFL
GFNWRYTRNN YGVPVKLDPG RSRDILSIKY TAIADSLKDH ASQLVNDGLV SV
//
