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Database: UniProt
Entry: A0A0Q8QP12_9BURK
LinkDB: A0A0Q8QP12_9BURK
Original site: A0A0Q8QP12_9BURK 
ID   A0A0Q8QP12_9BURK        Unreviewed;       292 AA.
AC   A0A0Q8QP12;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|ARBA:ARBA00017099, ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|ARBA:ARBA00012929, ECO:0000256|RuleBase:RU364082};
GN   ORFNames=ASE26_13010 {ECO:0000313|EMBL:KRB83383.1};
OS   Duganella sp. Root198D2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Duganella.
OX   NCBI_TaxID=1736489 {ECO:0000313|EMBL:KRB83383.1, ECO:0000313|Proteomes:UP000051728};
RN   [1] {ECO:0000313|EMBL:KRB83383.1, ECO:0000313|Proteomes:UP000051728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root198D2 {ECO:0000313|EMBL:KRB83383.1,
RC   ECO:0000313|Proteomes:UP000051728};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB83383.1, ECO:0000313|Proteomes:UP000051728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root198D2 {ECO:0000313|EMBL:KRB83383.1,
RC   ECO:0000313|Proteomes:UP000051728};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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|ARBA:ARBA00000079,
CC         ECO:0000256|RuleBase:RU364082};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU364082};
CC       Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000256|RuleBase:RU364082};
CC   -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004781, 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:KRB83383.1}.
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DR   EMBL; LMIC01000049; KRB83383.1; -; Genomic_DNA.
DR   RefSeq; WP_057247238.1; NZ_LMIC01000049.1.
DR   AlphaFoldDB; A0A0Q8QP12; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000051728; 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:UP000051728}.
FT   DOMAIN          1..291
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   292 AA;  30920 MW;  D4AB6B9BB2B12B9B CRC64;
     MKILLIGKNG QVGHELQRTL LPLGELVALG RDGLDLSDLT AVKQVLESQA ADVIVNASAY
     TAVDRAEADE AGAQAVNGAA VAAMAAYASA RNALLVHYST DYVFDGDKPA PYVEDDATAP
     QSAYGRSKRA GEEAIMASGC KALVFRTSWV FSAHGGNFIK TMLRLAGERD SLNVVADQFG
     APTSAELIAD VTALAVAAYR RSALAGGIYH LTAAGATSWH GLASYAIERA KVHGAALKVD
     PEQIKPIPTE AYPVPAKRPK NSRLDTSKLS TALDLQLPDW KIHVDRLIEQ LS
//
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