ID I3BKK3_BIFLN Unreviewed; 476 AA.
AC I3BKK3;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN ORFNames=HMPREF1312_2010 {ECO:0000313|EMBL:EIJ31896.1};
OS Bifidobacterium longum subsp. longum 44B.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1161743 {ECO:0000313|EMBL:EIJ31896.1, ECO:0000313|Proteomes:UP000004495};
RN [1] {ECO:0000313|EMBL:EIJ31896.1, ECO:0000313|Proteomes:UP000004495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=44B {ECO:0000313|EMBL:EIJ31896.1};
RX PubMed=23682142;
RA Shkoporov A.N., Efimov B.A., Khokhlova E.V., Chaplin A.V., Kafarskaya L.I.,
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Sutton G., Weibel D.B.,
RA Nelson K.E., Smeianov V.V.;
RT "Draft Genome Sequences of Two Pairs of Human Intestinal Bifidobacterium
RT longum subsp. longum Strains, 44B and 1-6B and 35B and 2-2B, Consecutively
RT Isolated from Two Children after a 5-Year Time Period.";
RL Genome Announc. 1:E00234-13(2013).
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}.
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:EIJ31896.1}.
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DR EMBL; AJTM01000014; EIJ31896.1; -; Genomic_DNA.
DR AlphaFoldDB; I3BKK3; -.
DR PATRIC; fig|1161743.3.peg.708; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000004495; 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; cd00438; cupin_RmlC; 1.
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 NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|RuleBase:RU364082};
KW Oxidoreductase {ECO:0000256|RuleBase:RU364082}.
FT DOMAIN 191..471
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 476 AA; 53159 MW; DC7A751FE278D972 CRC64;
MSLEFEKELK VTKTNIPGLL VFDLPVHGDN RGWFKENWQR AKMTALGLPD FGPVQNNISF
NAKKGVTRGI HAEPWDKYIS IATGEIFGAW VDLRPGDSFG QVFTTRLDPS KAIYVPRGVG
NSFQALQDGT AYTYLVNAHW SLEQKKTYTF VNLADPELNI QWPIPLEDSE RSEADLHHPM
LKDAKPMAPK RTMVFGSNGK LGRAIRRYAE SHGLHGFEYH DTDTFDIADA KAYAAINWDL
YGTIINAAAF TAVDEAETPG GRKNAWRTNV QGVKNLARIA TEHRITLVHI SSDYVFDGTK
ELHTEDEEFA PLGVYGQTKA AGDALVENVP QHYLLRSSWV IGEGRNFVTR MLGLAQNHAH
AEAPSDQFGR LTFTDDMANA IFHLLDCGAS YGTYNMTGSG RIASWYDIAR LVFQTAGVDP
DTITANSVAE YAREHHAAMR PQNCSLDLSK LEATGYHPQD WEQSLTTYLA KELEQR
//