ID I3E4B6_BACMT Unreviewed; 286 AA.
AC I3E4B6;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN ORFNames=PB1_00290 {ECO:0000313|EMBL:EIJ81337.1};
OS Bacillus methanolicus PB1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=997296 {ECO:0000313|EMBL:EIJ81337.1, ECO:0000313|Proteomes:UP000010523};
RN [1] {ECO:0000313|EMBL:EIJ81337.1, ECO:0000313|Proteomes:UP000010523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB1 {ECO:0000313|EMBL:EIJ81337.1,
RC ECO:0000313|Proteomes:UP000010523};
RX PubMed=22610424; DOI=10.1128/AEM.00703-12;
RA Heggeset T.M., Krog A., Balzer S., Wentzel A., Ellingsen T.E.,
RA Brautaset T.;
RT "Genome Sequence of Thermotolerant Bacillus methanolicus: Features and
RT Regulation Related to Methylotrophy and Production of L-Lysine and L-
RT Glutamate from Methanol.";
RL Appl. Environ. Microbiol. 78:5170-5181(2012).
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:EIJ81337.1}.
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DR EMBL; AFEU01000001; EIJ81337.1; -; Genomic_DNA.
DR AlphaFoldDB; I3E4B6; -.
DR STRING; 997296.PB1_00290; -.
DR PATRIC; fig|997296.3.peg.95; -.
DR eggNOG; COG1091; Bacteria.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000010523; 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}.
FT DOMAIN 7..282
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 286 AA; 32349 MW; 5A2C717C71486F22 CRC64;
MRIGESMDIL ITGGNGQLGK ELERQLSIAH SVISLGKQDL DITSKEDVEK IISNMKPQII
IHAAAFTAVD QCETDRKRAF EVNSLGAFYV AQAASKVGAR MFYLSSDYVF DGNKHSPYVE
EDEPNPQSIY GMSKWLGEKL VLLFDHVTVI RTSWLYGHDG KNFVKTMLEL AKKNREFKVV
NDQIGSPTYV YDLTETIIHL FDKKNGIYHV SNSGSCTWYV FAKTIFEEAG FNPKNVMPTT
TEEYGALAPR PRYSVLGHNA LLRENVNLPR PWKEALKDFL RKETGQ
//
