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Database: UniProt
Entry: F5LSM6_9BACL
LinkDB: F5LSM6_9BACL
Original site: F5LSM6_9BACL 
ID   F5LSM6_9BACL            Unreviewed;       280 AA.
AC   F5LSM6;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN   ORFNames=HMPREF9413_2030 {ECO:0000313|EMBL:EGL14009.1};
OS   Paenibacillus sp. HGF7.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=944559 {ECO:0000313|EMBL:EGL14009.1, ECO:0000313|Proteomes:UP000003445};
RN   [1] {ECO:0000313|EMBL:EGL14009.1, ECO:0000313|Proteomes:UP000003445}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HGF7 {ECO:0000313|EMBL:EGL14009.1,
RC   ECO:0000313|Proteomes:UP000003445};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (FEB-2011) 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|RuleBase:RU364082};
CC   -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC       {ECO:0000256|RuleBase:RU364082}.
CC   -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose reductase family.
CC       {ECO:0000256|ARBA:ARBA00010944, ECO:0000256|RuleBase:RU364082}.
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:EGL14009.1}.
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DR   EMBL; AFDH01000142; EGL14009.1; -; Genomic_DNA.
DR   RefSeq; WP_009676958.1; NZ_AFDH01000142.1.
DR   AlphaFoldDB; F5LSM6; -.
DR   OrthoDB; 9803892at2; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000003445; Unassembled WGS sequence.
DR   GO; GO:0008831; F:dTDP-4-dehydrorhamnose reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05254; dTDP_HR_like_SDR_e; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR005913; dTDP_dehydrorham_reduct.
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; PF04321; RmlD_sub_bind; 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:UP000003445}.
FT   DOMAIN          1..238
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   280 AA;  31136 MW;  D98DC3C9D9230D70 CRC64;
     MKLLVTGGQG MAGHVMVRYL RRLPGFQVAY TTRDGSDREG LLADARDTVR IRGIIETFRP
     DAVINCIGVL NQFAEADPVN AYRVNGIFPH DLAEAALGAG GRLIHISTDC VFSGRHGDHT
     EDDVPDGTSV YGRSKALGEV REAPHLTVRT SIIGPEIRES GIGLLHWFLS REGEVGGYTR
     AYWNGVTTLE LAKFVEHALQ RPELTGLVHL TAPVKVSKYE LLNLFRKQFG RTDIEVRKNA
     SVRLNRTLKN TRSDLNYAIP GYETMLKELD EWMCAQCLES
//
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