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Database: UniProt
Entry: A0A1X2CE19_9MYCO
LinkDB: A0A1X2CE19_9MYCO
Original site: A0A1X2CE19_9MYCO 
ID   A0A1X2CE19_9MYCO        Unreviewed;       286 AA.
AC   A0A1X2CE19;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN   Name=rmlD {ECO:0000313|EMBL:BBX65653.1};
GN   ORFNames=AWC23_06010 {ECO:0000313|EMBL:ORW74063.1}, MSAS_48270
GN   {ECO:0000313|EMBL:BBX65653.1};
OS   Mycobacterium saskatchewanense.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium simiae complex.
OX   NCBI_TaxID=220927 {ECO:0000313|EMBL:BBX65653.1, ECO:0000313|Proteomes:UP000467517};
RN   [1] {ECO:0000313|EMBL:ORW74063.1, ECO:0000313|Proteomes:UP000193387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44616 {ECO:0000313|EMBL:ORW74063.1,
RC   ECO:0000313|Proteomes:UP000193387};
RA   Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA   Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA   Olivier J., Enrico T., Nicola S.;
RT   "The new phylogeny of the genus Mycobacterium.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BBX65653.1, ECO:0000313|Proteomes:UP000467517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 13016 {ECO:0000313|EMBL:BBX65653.1,
RC   ECO:0000313|Proteomes:UP000467517};
RX   PubMed=31287781;
RA   Matsumoto Y., Kinjo T., Motooka D., Nabeya D., Jung N., Uechi K., Horii T.,
RA   Iida T., Fujita J., Nakamura S.;
RT   "Comprehensive subspecies identification of 175 nontuberculous mycobacteria
RT   species based on 7547 genomic profiles.";
RL   Emerg. Microbes Infect. 8:1043-1053(2019).
RN   [3] {ECO:0000313|EMBL:BBX65653.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 13016 {ECO:0000313|EMBL:BBX65653.1};
RA   Matsumoto Y., Motooka D., Nakamura S.;
RL   Submitted (FEB-2020) 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}.
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DR   EMBL; AP022573; BBX65653.1; -; Genomic_DNA.
DR   EMBL; LQPR01000011; ORW74063.1; -; Genomic_DNA.
DR   STRING; 220927.AWC23_06010; -.
DR   KEGG; msak:MSAS_48270; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000193387; Unassembled WGS sequence.
DR   Proteomes; UP000467517; Chromosome.
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          4..283
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   286 AA;  29329 MW;  ED6EC0A25F59F421 CRC64;
     MSARILITGA GGQLGGRLAA LTAEQGRDAQ AFTSSQWDIT DPAAAERVIR GGDVVINCAA
     YTNVDAAESD EAAAYAVNAT APGHLAKACD RVGARLIHVS TDFVFSGGAD PRPFEPSDDT
     DARGVYAQSK LAGERAVLAA SPGAVVVRTA WVYTGGTGRD FVAIMRRLAA GDGPVDVVDD
     QVGSPTYVGD LAVALLQVAD ANVAGPILHA ANEGAVSRFE LARAVFEECG ADPARVHPVS
     TAQFPRPAPR PTYSALGGRE SAAAGLTPLR DWRTALAAAL ADAHAI
//
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