ID M9LMV8_PAEPP Unreviewed; 279 AA.
AC M9LMV8;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN ORFNames=PPOP_0912 {ECO:0000313|EMBL:GAC41561.1};
OS Paenibacillus popilliae ATCC 14706.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1212764 {ECO:0000313|EMBL:GAC41561.1, ECO:0000313|Proteomes:UP000029453};
RN [1] {ECO:0000313|EMBL:GAC41561.1, ECO:0000313|Proteomes:UP000029453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14706 {ECO:0000313|EMBL:GAC41561.1,
RC ECO:0000313|Proteomes:UP000029453};
RA Iiyama K., Mori K., Mon H., Chieda Y., Lee J.M., Kusakabe T., Tashiro K.,
RA Asano S., Yasunaga-Aoki C., Shimizu S.;
RT "Draft Genome Sequence of Paenibacillus popilliae ATCC 14706T.";
RL Submitted (OCT-2012) 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:GAC41561.1}.
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DR EMBL; BALG01000040; GAC41561.1; -; Genomic_DNA.
DR RefSeq; WP_006284888.1; NZ_BALG01000040.1.
DR AlphaFoldDB; M9LMV8; -.
DR OrthoDB; 9803892at2; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000029453; 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 Reference proteome {ECO:0000313|Proteomes:UP000029453}.
FT DOMAIN 1..277
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 279 AA; 31423 MW; 630DF7A9C4908768 CRC64;
MKVLVTGATG QLGADVVRLF AEKGHHVMGM GRAQFDITDE KRCKDMITEV QPEAIIHCAA
YTAVDHAETD QNNAYLVNAI GTRNIAVAAE QVKAKMCYIS TDYVFDGNSS SPYYEYDNTN
PVTVYGKSKR AGEQLVQSLC SRWFIVRTSW VYGASGSNFV KTMVKLGAER DSLQVVNDQW
GSPTYTYDLS FFLEELVASE KYGIYHASNT GVCTWYEFAK AIFEEAKMAV KVDPCTTEQF
PRPAPRPRYS AMEPMAIRVN GFTPIRHWRE ALRDYLHQP
//
