ID A0A1Q2CHF5_9ACTN Unreviewed; 459 AA.
AC A0A1Q2CHF5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN ORFNames=RPIT_12650 {ECO:0000313|EMBL:AQP45549.1}, SAMN05428934_104156
GN {ECO:0000313|EMBL:SDY79342.1};
OS Tessaracoccus flavus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=1610493 {ECO:0000313|EMBL:AQP45549.1, ECO:0000313|Proteomes:UP000188324};
RN [1] {ECO:0000313|EMBL:AQP45549.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RP1T {ECO:0000313|EMBL:AQP45549.1};
RX PubMed=26869509; DOI=10.1099/ijsem.0.000958;
RA Kumari R., Singh P., Schumann P., Lal R.;
RT "Tessaracoccus flavus sp. nov., isolated from the drainage system of a
RT lindane-producing factory.";
RL Int. J. Syst. Evol. Microbiol. 66:1862-1868(2016).
RN [2] {ECO:0000313|EMBL:SDY79342.1, ECO:0000313|Proteomes:UP000199635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RP1 {ECO:0000313|EMBL:SDY79342.1,
RC ECO:0000313|Proteomes:UP000199635};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AQP45549.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RP1T {ECO:0000313|EMBL:AQP45549.1};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; CP019605; AQP45549.1; -; Genomic_DNA.
DR EMBL; FNPU01000004; SDY79342.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2CHF5; -.
DR STRING; 1610493.RPIT_12650; -.
DR KEGG; tfl:RPIT_12650; -.
DR OrthoDB; 9803892at2; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000188324; Chromosome.
DR Proteomes; UP000199635; 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 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 NADP {ECO:0000256|RuleBase:RU364082};
KW Oxidoreductase {ECO:0000256|RuleBase:RU364082};
KW Reference proteome {ECO:0000313|Proteomes:UP000188324}.
FT DOMAIN 187..457
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 459 AA; 49199 MW; 1616769634595F96 CRC64;
MTNELRVSTT DIPGLLVVDL PVHGDSRGWF KENWQRDKMT ALGVPDFQPV QNNMSFNADA
GVTRGIHAEP WDKLVSVATG RVFGAWVDLR AGETFGTVVT AELTPGRAVF VPRGVGNAYQ
ALDPGTCYSY LVNEHWSADA KAKYTFANLR HPDIRWPLPL DGATISEADR SHPSIADVVP
FRRPRPVVTG SNGQLGTALQ ALIPEAIFVD RADLDITDAD AVAAFDWSEA SCIINAAAWT
AVDAAEGEGR AACWAVNVAG TANLVAAARR HRLPLVHISS DYVFDGSREL HTEDEPFAPL
SAYGAAKAAA DAVVGTLPRH YILRTSWVIG EGSNFVRTMA RLADTGASPA VVDDQFGRLT
FADDLARAAL HLMHHAEPGT YNVTSDGGVV SWFDVAQAVF EARGAAGQVS RTSTEEFAAG
KLTAPRPRHS ALDLTKLRAT GFVPVDGGEG LRQYLAAMT
//
