ID   A0A1I4YJF6_9PROT        Unreviewed;       755 AA.
AC   A0A1I4YJF6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|ARBA:ARBA00017099, ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|ARBA:ARBA00012929, ECO:0000256|RuleBase:RU364082};
GN   ORFNames=SAMN05216386_0731 {ECO:0000313|EMBL:SFN38171.1};
OS   Nitrosospira briensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=35799 {ECO:0000313|EMBL:SFN38171.1, ECO:0000313|Proteomes:UP000183107};
RN   [1] {ECO:0000313|Proteomes:UP000183107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nsp8 {ECO:0000313|Proteomes:UP000183107};
RA   Varghese N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to
CC       yield dTDP-L-rhamnose. {ECO:0000256|RuleBase:RU364082}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-
CC         rhamnose + H(+) + NADPH; Xref=Rhea:RHEA:21796, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57510, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:62830; EC=1.1.1.133;
CC         Evidence={ECO:0000256|ARBA:ARBA00000079,
CC         ECO:0000256|RuleBase:RU364082};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU364082};
CC       Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000256|RuleBase:RU364082};
CC   -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004781, ECO:0000256|RuleBase:RU364082}.
CC   -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose reductase family.
CC       {ECO:0000256|ARBA:ARBA00010944, ECO:0000256|RuleBase:RU364082}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FOVJ01000001; SFN38171.1; -; Genomic_DNA.
DR   RefSeq; WP_074794740.1; NZ_FOVJ01000001.1.
DR   AlphaFoldDB; A0A1I4YJF6; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000183107; Unassembled WGS sequence.
DR   GO; GO:0008831; F:dTDP-4-dehydrorhamnose reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05254; dTDP_HR_like_SDR_e; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 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; IPR005913; dTDP_dehydrorham_reduct.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR029903; RmlD-like-bd.
DR   PANTHER; PTHR10491; DTDP-4-DEHYDRORHAMNOSE REDUCTASE; 1.
DR   PANTHER; PTHR10491:SF4; METHIONINE ADENOSYLTRANSFERASE 2 SUBUNIT BETA; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   Pfam; PF04321; RmlD_sub_bind; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|RuleBase:RU364082};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364082};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183107}.
FT   DOMAIN          460..714
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
FT   REGION          735..755
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   755 AA;  84644 MW;  004A249F9EE045FB CRC64;
     MSGEEDQGAT EALELWGGLE CTVNRVLDTY FSQMDRNGHI HRLCDLERFA SLGIRSIRYP
     VLWEHMAPDG LDRIDWSWPD DRLPALRERG ITPIVGLVHH GSGPQYTSLV DPGFAEKLAV
     FAGAVAQRYP WVEHYTPVNE PLTTARFSGL YGLWYPHGSD ERTFVQALLN QCRAVVLSMR
     AIRQVNPDAK LVQTDDLGKA YSTPQLSGLA EFYNARRWLA WDLLCGKVGQ EHPLWNYLVG
     TGIEPSQVLW FKDNVCHPEI IGINYYITSE RWLDERVERY PGQHITDYHG YRFVDMEPVR
     VLATPSTGVE HLLTEAWERY RLPLAITEVH IGASREDQMR WLLEMWQAAR NARQRGIDIR
     AVTVWALLGS YDWNCLVTAC KGYYEPGPFD VRSALPRPTA VAGLMRELAA GRQPSHPVLK
     GQGWWRRADR LTCKPVATPT AITSLHSKYK SSVNGTMRPI LVTGATGTLG RAFAIICGKR
     NVAGILLSRQ EMDIAVRASV ECAVARYQPW AIINASGYVN VDNAESDIDR CFRENAVGPS
     VLAALCRERD IQLLTFSSDL VFDGRQASPY RESDTVCPLN HYGRSKVEAE RRVLDHHPDA
     LVVRTSAFFG PWDIYNFVTL ALKTLAQEER FSASTDITVS PTYVPDLVNT CLDLLIDKEA
     GIWHLTNGEP VTWVELALKA AKKAGIDTSR LDGRCGNELG YVAVRPLYSA LSSERGILLP
     SLDDALDRYI ESRRQEASAE AEQNKSGRRG SGMVA
//