ID A0A380NMU6_9FIRM Unreviewed; 305 AA.
AC A0A380NMU6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN Name=rmlD {ECO:0000313|EMBL:SUP44772.1};
GN ORFNames=NCTC12020_01824 {ECO:0000313|EMBL:SUP44772.1};
OS Veillonella criceti.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=103891 {ECO:0000313|EMBL:SUP44772.1, ECO:0000313|Proteomes:UP000255367};
RN [1] {ECO:0000313|EMBL:SUP44772.1, ECO:0000313|Proteomes:UP000255367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12020 {ECO:0000313|EMBL:SUP44772.1,
RC ECO:0000313|Proteomes:UP000255367};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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; UHIO01000001; SUP44772.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A380NMU6; -.
DR OrthoDB; 9803892at2; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000255367; 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 Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR InterPro; IPR005913; dTDP_dehydrorham_reduct.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029903; RmlD-like-bd.
DR NCBIfam; TIGR01214; rmlD; 1.
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 ECO:0000313|EMBL:SUP44772.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000255367}.
FT DOMAIN 1..297
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 305 AA; 34421 MW; E69AE2341B1FE77D CRC64;
MKILITGVTG QLGYDVAVEA LSRAHEVIGI SRRAYTINNT RYKNFICSIT DEAKIKEVFT
AVKPDVVIHC AAWTAVDAAE ESENKDILYK TNVEATKYIS KCCEVIDAKL IYISTDYVFD
GQGTAIWQEA EQNLHPINLY GESKLLGEQA ILSALKKYFI VRISWVFGIN GNNFVKTMLS
VGQKYDSLKV VNDQIGLPTY TKDLAGLLLD MAESTSYGIY HATNTGSYIS WYDFAKEIFK
QANYQTNVIP VTTDEYGISK ANRPKNSRLS LNRLSDNGFT LLPNWKDALQ RYLQELRNED
EINKN
//
