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Database: UniProt
Entry: I3BKK3_BIFLN
LinkDB: I3BKK3_BIFLN
Original site: I3BKK3_BIFLN 
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
//
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