ID A0A368VDQ2_9ACTN Unreviewed; 305 AA.
AC A0A368VDQ2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN ORFNames=DFQ14_11728 {ECO:0000313|EMBL:RCW39192.1};
OS Halopolyspora algeriensis.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetes incertae sedis;
OC Halopolyspora.
OX NCBI_TaxID=1500506 {ECO:0000313|EMBL:RCW39192.1, ECO:0000313|Proteomes:UP000253495};
RN [1] {ECO:0000313|EMBL:RCW39192.1, ECO:0000313|Proteomes:UP000253495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8575 {ECO:0000313|EMBL:RCW39192.1,
RC ECO:0000313|Proteomes:UP000253495};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUL-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 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:RCW39192.1}.
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DR EMBL; QPJC01000017; RCW39192.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368VDQ2; -.
DR OrthoDB; 9803892at2; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000253495; 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:UP000253495}.
FT DOMAIN 6..295
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 305 AA; 32885 MW; 52A13DBF0AD43C8F CRC64;
MPRLAVLVPG GRGQLGRELA RIVDADRNGL VHAPGSTELD VADPGAVTDA VDSFAEAARD
ARLQPVVINA AAYTAVDAAE SDRDRAAEVN TRGAAHLAEA CAVSDAPLVH VSTDYVFAGD
AREPYEPDHP TGPYTVYGRT KLDGEHAVLD SRARAWVVRT SWVYGAQGGN FVKTMARLES
ERETVSVVDD QIGSPTWAGD LARGLVELAD RAAREQGPGR RILHCTNSGR TSWFEFARAV
FTELGADPDR VHSCSTAEFP RPAPRPAFSV LSERAWIEEG CTPMRPWREA LAEAFVRDGG
ALRAR
//