ID A0A1T4WM21_9FIRM Unreviewed; 280 AA.
AC A0A1T4WM21;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN ORFNames=SAMN02745178_00761 {ECO:0000313|EMBL:SKA78259.1};
OS Gemmiger formicilis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Gemmiger.
OX NCBI_TaxID=745368 {ECO:0000313|EMBL:SKA78259.1, ECO:0000313|Proteomes:UP000190286};
RN [1] {ECO:0000313|EMBL:SKA78259.1, ECO:0000313|Proteomes:UP000190286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27749 {ECO:0000313|EMBL:SKA78259.1,
RC ECO:0000313|Proteomes:UP000190286};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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}.
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DR EMBL; FUYF01000003; SKA78259.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4WM21; -.
DR STRING; 745368.SAMN02745178_00761; -.
DR OrthoDB; 9808602at2; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000190286; 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 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:UP000190286}.
FT DOMAIN 3..231
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 280 AA; 30951 MW; E68A060B41865527 CRC64;
MKKLLVSGAG GFVGARIMTQ LAGRYELCAF PKGMLAAADE QTVADWVRRE QPDVIVHTAA
LSDTGYSEKH PDESYRANVL LPCWMAAAAQ KSGARLVAFS SDQVYTGLTE HGPFDEDIPL
SPANVYGRHK QEMEQRVLDI LPDAVLLRAA WMYDLPGYGL PIRGNFLLNL LTAAMRQETL
RFSARDYRGI TYVREAVERL TQAMELPGGV YNFGSENDCD MVTTARRACA LLDIHPVIET
ADWPRSLLMD GGRFRAAAGV GFDDTLTGVQ RCLRDYGLLK
//
