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Database: UniProt
Entry: A0A0Q8Q8P2_9ACTN
LinkDB: A0A0Q8Q8P2_9ACTN
Original site: A0A0Q8Q8P2_9ACTN 
ID   A0A0Q8Q8P2_9ACTN        Unreviewed;       450 AA.
AC   A0A0Q8Q8P2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN   ORFNames=ASE01_06010 {ECO:0000313|EMBL:KRB78217.1};
OS   Nocardioides sp. Root190.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1736488 {ECO:0000313|EMBL:KRB78217.1, ECO:0000313|Proteomes:UP000050886};
RN   [1] {ECO:0000313|EMBL:KRB78217.1, ECO:0000313|Proteomes:UP000050886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root190 {ECO:0000313|EMBL:KRB78217.1,
RC   ECO:0000313|Proteomes:UP000050886};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB78217.1, ECO:0000313|Proteomes:UP000050886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root190 {ECO:0000313|EMBL:KRB78217.1,
RC   ECO:0000313|Proteomes:UP000050886};
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|RuleBase:RU364082};
CC   -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC       {ECO:0000256|RuleBase:RU364082}.
CC   -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family.
CC       {ECO:0000256|ARBA:ARBA00010154}.
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:KRB78217.1}.
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DR   EMBL; LMIA01000008; KRB78217.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q8Q8P2; -.
DR   STRING; 1736488.ASE01_06010; -.
DR   OrthoDB; 9803892at2; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000050886; Unassembled WGS sequence.
DR   GO; GO:0008830; F:dTDP-4-dehydrorhamnose 3,5-epimerase activity; IEA:InterPro.
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; 2.60.120.10; Jelly Rolls; 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; IPR000888; RmlC-like.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   InterPro; IPR029903; RmlD-like-bd.
DR   PANTHER; PTHR10491; DTDP-4-DEHYDRORHAMNOSE REDUCTASE; 1.
DR   PANTHER; PTHR10491:SF4; METHIONINE ADENOSYLTRANSFERASE 2 SUBUNIT BETA; 1.
DR   Pfam; PF00908; dTDP_sugar_isom; 1.
DR   Pfam; PF04321; RmlD_sub_bind; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF51182; RmlC-like cupins; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|RuleBase:RU364082};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364082};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050886}.
FT   DOMAIN          171..445
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
FT   ACT_SITE        53
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600888-1"
FT   ACT_SITE        116
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600888-1"
FT   SITE            122
FT                   /note="Participates in a stacking interaction with the
FT                   thymidine ring of dTDP-4-oxo-6-deoxyglucose"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600888-3"
SQ   SEQUENCE   450 AA;  48777 MW;  93D3865CC2451D30 CRC64;
     MLVLRLDVHR DDRGWFKENW QRARMVEAGL PDFGPVQNNM SLNAQRGVTR GIHAEPWDKL
     VSVAIGKVFA AWVDLRPGEH FGATYWTEID ENVAVFVPRG VGNAYQALVD GTVYSYLVND
     HYSPGTTYPA LDLADETVAI PWPIPLAEAE TSEKDLTNPS LAEVTPMPPK RTLITGCRGQ
     LGQALAREFP DATLVDLDEL DLTDPKALEA WPWQEYGVVL NAAAYTAVDR AETPEGRADA
     WAANAAAPAA LARIAARRGL TLVHYSTDYV FDGSEVPGGH AEDEPFAPLG VYGQTKAAGD
     IAVATAPRHY VLRTSWVIGE GHNFVRTMQK LAADGVDPAV VDDQVGRLTF TDELARATRH
     LLDTGAAHGT YNVTNSGVPR SWADYARCVF ELTGHDPARV STVTSEEYAA GKSLSPRPLH
     STLCLDKLAA TGFVSRDAEV ALADYTTPLG
//
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