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Database: UniProt
Entry: A0A1A2GJA1_9MYCO
LinkDB: A0A1A2GJA1_9MYCO
Original site: A0A1A2GJA1_9MYCO 
ID   A0A1A2GJA1_9MYCO        Unreviewed;       311 AA.
AC   A0A1A2GJA1;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN   ORFNames=A5764_20910 {ECO:0000313|EMBL:OBG29481.1};
OS   Mycobacterium sp. 852002-51057_SCH5723018.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1834094 {ECO:0000313|EMBL:OBG29481.1, ECO:0000313|Proteomes:UP000092171};
RN   [1] {ECO:0000313|Proteomes:UP000092171}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=852002-51057_SCH5723018 {ECO:0000313|Proteomes:UP000092171};
RA   Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Mehaffy C., Tameris M.,
RA   Hatherill M., Hanekom W., Mahomed H., Mcshane H.;
RL   Submitted (JUN-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 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:OBG29481.1}.
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DR   EMBL; LZIR01000008; OBG29481.1; -; Genomic_DNA.
DR   RefSeq; WP_067108000.1; NZ_LZIR01000008.1.
DR   AlphaFoldDB; A0A1A2GJA1; -.
DR   STRING; 1834094.A5764_20910; -.
DR   OrthoDB; 9803892at2; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000092171; 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}.
FT   DOMAIN          8..292
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
FT   REGION          292..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   311 AA;  32415 MW;  847F41DE98C4CDA8 CRC64;
     MSGRSTRFVI SGAGGQLGGC LAAMATNQGR DALALTSSQW DITDPAAAER IIRAGDVVIN
     CAAYTNVDGA ESDEAAAYAV NATGPEHIAR ACARAGARLI HVSTDFVFFG DRADFNGDPP
     RPFEPSDETD ARGVYARSKL AGERAVLEAQ PEAVVVRTAW VYTGGTGKDF VAVMRRLAAG
     DGPVNVVDDQ TGSPTYVADL AAALLQVADD HVPGPILHAA NEGAVSRFEQ TRAIFSECGA
     DPARVRPVST AEFPRPAPRP IYSALGSRES AAAGLVPLRP WRTALVAALA AAQTNESTDA
     SADRPLPSTR D
//
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