ID L1NFF1_9PORP Unreviewed; 293 AA.
AC L1NFF1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 13-SEP-2023, entry version 35.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN ORFNames=HMPREF9134_00613 {ECO:0000313|EMBL:EKY02224.1};
OS Porphyromonas catoniae F0037.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1127696 {ECO:0000313|EMBL:EKY02224.1, ECO:0000313|Proteomes:UP000010408};
RN [1] {ECO:0000313|EMBL:EKY02224.1, ECO:0000313|Proteomes:UP000010408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0037 {ECO:0000313|EMBL:EKY02224.1,
RC ECO:0000313|Proteomes:UP000010408};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (MAY-2012) 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:EKY02224.1}.
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DR EMBL; AMEQ01000018; EKY02224.1; -; Genomic_DNA.
DR RefSeq; WP_005468814.1; NZ_KB291043.1.
DR AlphaFoldDB; L1NFF1; -.
DR STRING; 1127696.HMPREF9134_00613; -.
DR PATRIC; fig|1127696.3.peg.542; -.
DR eggNOG; COG1091; Bacteria.
DR HOGENOM; CLU_045518_1_2_10; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000010408; 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}.
FT DOMAIN 5..286
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 293 AA; 33319 MW; 3F3797C696997CBC CRC64;
MGKSNILVLG AGGQLGQELR AVAEGSVQHY FFMSRSELDV TDQLAVKLFV QKHRIDTIVN
CSAYTAVDRA EDEAEEADRI NHRAVAGLAE LAKECGLYLI HISTDYVFRG DSHLPITEDE
IPCPQSVYGR TKLLGEEAIR HTGCHALILR TSWLYSTYGS NFVKTMCRLM QEREELSVVF
DQIGTPTYAR DLALFLVFTL DQNVGCRHEG TYHFADEGVC SWYDFAEAIR HYMGYHCRLC
PIRSDQYPTK AMRPSYSVLD KSKLKRAFGV TLPHWQTSLE ECLRKLTWTD TNE
//
