ID A0A139NLH5_9STRE Unreviewed; 283 AA.
AC A0A139NLH5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN ORFNames=STRDD12_00034 {ECO:0000313|EMBL:KXT76900.1};
OS Streptococcus sp. DD12.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1777880 {ECO:0000313|EMBL:KXT76900.1, ECO:0000313|Proteomes:UP000070638};
RN [1] {ECO:0000313|EMBL:KXT76900.1, ECO:0000313|Proteomes:UP000070638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD12 {ECO:0000313|EMBL:KXT76900.1,
RC ECO:0000313|Proteomes:UP000070638};
RA Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I.,
RA Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.;
RT "Highly variable Streptococcus oralis are common among viridans
RT streptococci isolated from primates.";
RL Submitted (JAN-2016) 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:KXT76900.1}.
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DR EMBL; LQRG01000001; KXT76900.1; -; Genomic_DNA.
DR RefSeq; WP_066913770.1; NZ_KQ969495.1.
DR AlphaFoldDB; A0A139NLH5; -.
DR STRING; 1777880.STRDD12_00034; -.
DR PATRIC; fig|1777880.3.peg.34; -.
DR OrthoDB; 9803892at2; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000070638; 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 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,
KW ECO:0000313|EMBL:KXT76900.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070638}.
FT DOMAIN 2..280
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 283 AA; 32227 MW; E7C66D2B7A082F6C CRC64;
MILITGAKGQ LGTELRYLLD ERNEDYVAVD VAEMDITDAE KVEQVFAEVK PTLVYHCAAY
TAVDAAEDEG KELDFAINVT GTENIAKAAA KYDATLVYIS TDYVFDGEKP VGQEWEVDDQ
PDPQTEYGRT KRMGEELVEK YAKNFYIIRT AWVFGNYGKN FVFTMQNLAK THKTLTVVDD
QHGRPTWTRT LAEFMTYLAE NQKDFGYYHL SNDASEDTTW YDFAVEILKD TDVEVKPVDS
SQFPAKAKRP LNSTMSLKKA KATGFVIPTW QEALKEFYKQ DVK
//
