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Database: UniProt
Entry: A0A086BPI8_9BIFI
LinkDB: A0A086BPI8_9BIFI
Original site: A0A086BPI8_9BIFI 
ID   A0A086BPI8_9BIFI        Unreviewed;       484 AA.
AC   A0A086BPI8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE            EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN   ORFNames=BBOMB_1260 {ECO:0000313|EMBL:KFF31852.1};
OS   Bifidobacterium bombi DSM 19703.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1341695 {ECO:0000313|EMBL:KFF31852.1, ECO:0000313|Proteomes:UP000028730};
RN   [1] {ECO:0000313|EMBL:KFF31852.1, ECO:0000313|Proteomes:UP000028730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19703 {ECO:0000313|EMBL:KFF31852.1,
RC   ECO:0000313|Proteomes:UP000028730};
RX   PubMed=25085493; DOI=10.1128/AEM.02308-14;
RA   Milani C., Lugli G.A., Duranti S., Turroni F., Bottacini F., Mangifesta M.,
RA   Sanchez B., Viappiani A., Mancabelli L., Taminiau B., Delcenserie V.,
RA   Barrangou R., Margolles A., van Sinderen D., Ventura M.;
RT   "Genomic encyclopedia of type strains of the genus Bifidobacterium.";
RL   Appl. Environ. Microbiol. 80:6290-6302(2014).
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:KFF31852.1}.
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DR   EMBL; ATLK01000001; KFF31852.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A086BPI8; -.
DR   STRING; 1341695.BBOMB_1260; -.
DR   eggNOG; COG1091; Bacteria.
DR   eggNOG; COG1898; Bacteria.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000028730; 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; 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   Isomerase {ECO:0000313|EMBL:KFF31852.1};
KW   NADP {ECO:0000256|RuleBase:RU364082};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364082};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028730}.
FT   DOMAIN          191..480
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   484 AA;  53694 MW;  60E3914314CD6024 CRC64;
     MPFEFEKELK VTKTKHSRAF GLRPAGAWRQ PRLVQGKLAA RKMTALGLPD FGPVQNNISY
     NEKKGVTRGI HAEPWDKYIS IAAGEIFGAW VDLRSGESFG QVFTTRLDPS RAIFVPRGVG
     NSFQALQDGT VYTYLVNAHW SLEQKKTYTF VNLADPDLGI EWPIPLEQSE RSEADLHHPM
     LKDAKPMAPR RTLVTGANGQ LGQAIEQYVR RHGLQGFEFT DRDEFDFSDS KAYEAYDWSL
     YGTIINAGAY TAVDKAETDE GRVAAWKANA QGPALLARVA TEHNITLVHV SSDYVFDGTT
     EEHTETEPFS PLGVYGQSKA AGDIAVSNSP RHYILRSSWV IGQGHNFVNT MMELSNRVAD
     PNDTFNAVTV VNDQYGRLTF TDDMAEAIFH LLNSGAAYGT YNLTGSGAVR SWAEIAAEVF
     DKTNGNGDKV KPVSTADYYA RSTSLVSPRP RNSALNLSKI EHAGYRPADW EQSLQDYMNE
     KSGR
//
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