ID A0A383S8U4_9ACTN Unreviewed; 474 AA.
AC A0A383S8U4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, 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=D7U36_11315 {ECO:0000313|EMBL:RLP07099.1}, PROPAUS_1752
GN {ECO:0000313|EMBL:SYZ33799.1};
OS Propionibacterium australiense.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Propionibacterium.
OX NCBI_TaxID=119981 {ECO:0000313|EMBL:SYZ33799.1, ECO:0000313|Proteomes:UP000263928};
RN [1] {ECO:0000313|Proteomes:UP000263928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hornung B.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SYZ33799.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Propionibacterium_australiense1 {ECO:0000313|EMBL:SYZ33799.1};
RA Ferrada E.E., Latorre B.A.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:RLP07099.1, ECO:0000313|Proteomes:UP000279336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML98A078 {ECO:0000313|EMBL:RLP07099.1,
RC ECO:0000313|Proteomes:UP000279336};
RA Bernier A.-M., Bernard K.;
RT "Propionibacterium australiense Genome Sequencing and Assembly.";
RL Submitted (OCT-2018) 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; RCIW01000019; RLP07099.1; -; Genomic_DNA.
DR EMBL; UNQJ01000012; SYZ33799.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A383S8U4; -.
DR OrthoDB; 9803892at2; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000263928; Unassembled WGS sequence.
DR Proteomes; UP000279336; 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 Isomerase {ECO:0000313|EMBL:SYZ33799.1};
KW NADP {ECO:0000256|RuleBase:RU364082};
KW Oxidoreductase {ECO:0000256|RuleBase:RU364082};
KW Reference proteome {ECO:0000313|Proteomes:UP000263928}.
FT DOMAIN 191..470
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
FT ACT_SITE 71
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600888-1"
FT ACT_SITE 134
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600888-1"
FT SITE 140
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 474 AA; 51269 MW; A838A3F4BD4F1BB7 CRC64;
MTLEYSKQLD VRSTPIPDLL VIDLTVHGDS RGWFKENWQR AKMSALGLPD FGPVQNNISF
NDAVGVTRGI HAEPWDKFVS LATGRVFGAW VDLRAGNSFG TVFTCEIDPG TAVFVPRGVG
NAYQTLEPDT AYSYLVNDHW SPDAEYTFLN LADETAAIDW PIPLGKAILS DKDKTHPRLA
MVKPFPPRIP RVLVTGCRGQ LGRALMKQLA ASGFEPIGVD LDELNISDRA AVDAYDWSGI
DVIINAAAWT DVDGAETAEG RPRAWAANAI GPANLARTAS AHGIVLVHVS SEYIFDGTKS
LHAEDEPPSP LSVYGQSKAG GDAAVAAVPR HYLVRTSWVV GDGRNFVRTM ADLAARGVAP
SVVDDQIGRL TFTADLAAGI IHLLRTGAEF GTYNLSCEGE VVSWAHVAKR VYELTGHDPA
DVKPVTTEEY FAGKQAAPRP ADSSLNLSKL EATGFTPAVW DQRITEYLHA HRPA
//
