ID   X4ZIH2_9BACL            Unreviewed;       289 AA.
AC   X4ZIH2;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN   ORFNames=PSAB_21910 {ECO:0000313|EMBL:AHV99271.1};
OS   Paenibacillus sabinae T27.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1268072 {ECO:0000313|EMBL:AHV99271.1, ECO:0000313|Proteomes:UP000019772};
RN   [1] {ECO:0000313|EMBL:AHV99271.1, ECO:0000313|Proteomes:UP000019772}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T27 {ECO:0000313|EMBL:AHV99271.1,
RC   ECO:0000313|Proteomes:UP000019772};
RX   PubMed=24651173;
RA   Xie J.B., Du Z., Bai L., Tian C., Zhang Y., Xie J.Y., Wang T., Liu X.,
RA   Chen X., Cheng Q., Chen S., Li J.;
RT   "Comparative Genomic Analysis of N2-Fixing and Non-N2-Fixing Paenibacillus
RT   spp.: Organization, Evolution and Expression of the Nitrogen Fixation
RT   Genes.";
RL   PLoS Genet. 10:E1004231-E1004231(2014).
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; CP004078; AHV99271.1; -; Genomic_DNA.
DR   RefSeq; WP_025336722.1; NZ_CP004078.1.
DR   AlphaFoldDB; X4ZIH2; -.
DR   STRING; 1268072.PSAB_21910; -.
DR   KEGG; psab:PSAB_21910; -.
DR   PATRIC; fig|1268072.3.peg.4514; -.
DR   eggNOG; COG1091; Bacteria.
DR   HOGENOM; CLU_045518_1_2_9; -.
DR   OrthoDB; 9803892at2; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000019772; Chromosome.
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          4..287
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   289 AA;  32148 MW;  D15D1896C12B08A4 CRC64;
     MAGKVLVTGA TGQLGQDVVK LLEKQGHEVL ACDRQEMDIT DLDQCSKVIG EFGPEAIIHC
     AAHTAVDAAE TDIDAAYLIN AVGTRNVVVA AEKVGAKLVY ISTDYVFDGQ GSQPYHEYDN
     TDPKSIYGKS KRAGEILVQT LSSKYFIVRT SWVYGKYGNN FVKTMLKFGQ EKPVLQVVDD
     QKGSPTYTVD LANFLLELIG TEKYGIYHAS NTEVCTWYEF TQAIFAEAEE ILGLKFTAKL
     EPCTTEQFLR PAPRPRNSAM EHLSIRTNGF KDLRPWREGL KAFLAELRD
//