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Database: UniProt
Entry: A7LX67_BACO1
LinkDB: A7LX67_BACO1
Original site: A7LX67_BACO1 
ID   A7LX67_BACO1            Unreviewed;       303 AA.
AC   A7LX67;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN   ORFNames=BACOVA_02428 {ECO:0000313|EMBL:EDO11928.1};
OS   Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 /
OS   CCUG 4943 / NCTC 11153).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=411476 {ECO:0000313|EMBL:EDO11928.1, ECO:0000313|Proteomes:UP000005475};
RN   [1] {ECO:0000313|EMBL:EDO11928.1, ECO:0000313|Proteomes:UP000005475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC
RC   11153 {ECO:0000313|Proteomes:UP000005475};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDO11928.1, ECO:0000313|Proteomes:UP000005475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC
RC   11153 {ECO:0000313|Proteomes:UP000005475};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Bacteroides ovatus (ATCC 8483).";
RL   Submitted (APR-2007) 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:EDO11928.1}.
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DR   EMBL; AAXF02000048; EDO11928.1; -; Genomic_DNA.
DR   RefSeq; WP_004295770.1; NZ_DS264553.1.
DR   AlphaFoldDB; A7LX67; -.
DR   GeneID; 29453253; -.
DR   eggNOG; COG1091; Bacteria.
DR   HOGENOM; CLU_045518_2_1_10; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000005475; 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   InterPro; IPR005913; dTDP_dehydrorham_reduct.
DR   InterPro; IPR036291; NAD(P)-bd_dom_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; 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          3..296
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
SQ   SEQUENCE   303 AA;  34315 MW;  64DF1F1681C55ADB CRC64;
     MKKILIIGAN GFTGRQIVND LSACKQYKLT GCSLHPDILP NNAEDYRFIE TDIRNEADVR
     HLFKEVQPDV VINCSALSVP DYCETHHEEA YLTNVTAVGQ LADLCEEYKS RFIHLSTDFV
     FDGKINEAAG LLYTEKDLPA PINYYGYTKW KGEERVTETC SSYAIVRVEI VYGKALPGQH
     GNIVQLVMNR LKAGQEIRVV SDQWRTPTYV GDVSDGVLRL IEHTANGIFH ICGDECMTIA
     EIAYQVADYM KLDRSLIHPA TTEKMNESTP RPRFSGMSID KARTMLGYRP QKLKEILVNW
     DKL
//
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