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Database: UniProt
Entry: A0A1G9HH52_9ACTN
LinkDB: A0A1G9HH52_9ACTN
Original site: A0A1G9HH52_9ACTN 
ID   A0A1G9HH52_9ACTN        Unreviewed;       469 AA.
AC   A0A1G9HH52;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN   ORFNames=SAMN04488242_0282 {ECO:0000313|EMBL:SDL11833.1};
OS   Tessaracoccus oleiagri.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Tessaracoccus.
OX   NCBI_TaxID=686624 {ECO:0000313|EMBL:SDL11833.1, ECO:0000313|Proteomes:UP000199475};
RN   [1] {ECO:0000313|EMBL:SDL11833.1, ECO:0000313|Proteomes:UP000199475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.9159 {ECO:0000313|EMBL:SDL11833.1,
RC   ECO:0000313|Proteomes:UP000199475};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNGP01000001; SDL11833.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9HH52; -.
DR   STRING; 686624.SAMN04488242_0282; -.
DR   OrthoDB; 9803892at2; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000199475; 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; cd00438; cupin_RmlC; 1.
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:UP000199475}.
FT   DOMAIN          187..465
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
FT   ACT_SITE        67
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600888-1"
FT   ACT_SITE        130
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600888-1"
FT   SITE            136
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   469 AA;  51564 MW;  B944D2FFE0DEB80F CRC64;
     MSADLRIEGT PIEGLLLVHL PLHGDARGWF KEHWHRSKMT ALGLPDFKPV QQNVSFNADR
     GTTRGLHAEP WDKYVSVVNG SAFGAWVDLR EGASFGTLFT AELRPDTAVF VPRGVANGFQ
     TLEADTNYSY LVNDHWSPNA EYALVNLADP ALSIQWPIPL DDATISEKDR LHPELREITP
     VPPKKTAVLG SDGQLGRAIR VQLGATHIDY LTRDDLDLTD SHAIERHDWS GVGAIINAAA
     YTAVDGAETH DGRRHAWQIN STAVRDLARV CIQHDITLVH ISTDYVFDGE ELEHPEGESL
     SPLNNYGASK AAGELAASLV PKHYILRTSW VVGDGNNFVR TMAKLARDGV EASVIADQYG
     RLTFAEDLAG VIQSLLSGRQ PWGVYNVTSG GPLRTWYEIA TEVYSLLGVD PSMVSPITAA
     DYAAQRRAVA PHAERPRYSG LPMDELQRLG IAPSHEDAHL RRYLKGLHD
//
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