ID A0A0F0KB68_9MICO Unreviewed; 471 AA.
AC A0A0F0KB68;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN Name=rfbC {ECO:0000313|EMBL:KJL18123.1};
GN ORFNames=RN50_03230 {ECO:0000313|EMBL:KJL18123.1};
OS Microbacterium foliorum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=104336 {ECO:0000313|EMBL:KJL18123.1, ECO:0000313|Proteomes:UP000033572};
RN [1] {ECO:0000313|EMBL:KJL18123.1, ECO:0000313|Proteomes:UP000033572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12966 {ECO:0000313|EMBL:KJL18123.1,
RC ECO:0000313|Proteomes:UP000033572};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) 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 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:KJL18123.1}.
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DR EMBL; JYIU01000046; KJL18123.1; -; Genomic_DNA.
DR RefSeq; WP_045255469.1; NZ_JYIU01000046.1.
DR AlphaFoldDB; A0A0F0KB68; -.
DR KEGG; mfol:DXT68_06060; -.
DR PATRIC; fig|104336.4.peg.3271; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000033572; 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 Isomerase {ECO:0000313|EMBL:KJL18123.1};
KW NADP {ECO:0000256|RuleBase:RU364082};
KW Oxidoreductase {ECO:0000256|RuleBase:RU364082};
KW Reference proteome {ECO:0000313|Proteomes:UP000033572}.
FT DOMAIN 190..470
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
FT ACT_SITE 72
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600888-1"
FT ACT_SITE 135
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600888-1"
FT SITE 141
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 471 AA; 50844 MW; 6CD28A361A2AAC2A CRC64;
MAEIAFGKKL GIVETGIPGL VVFDLPVHGD SRGWFKENWQ REKMTALGLD DFGPVQNNIS
FNDAVGTTRG IHAEPWDKWV SVATGRIFGA WVDLREGPTF GAVFTAEIDP SKAIFVPRGV
GNSYQTLEPD TAYAYLVNDH WSPEASYSFL NLADETAAIA WPIDLADVEI SEKDLAHPRL
ADVTPISAKK ILVVGSGGQL GRALRDEFGA ADHIEWTTRA EFDLGDSELR TARRWRDYDA
IVNAGAYTAV DLAETAEGRR DAWAANASGP ARLASIAAEY GVTLVHVSSD YVFDGTSTRA
YLEDNVLCPL GVYGQSKAAG DLAVATAPRH YILRTSWVIG DGKNFVRTMA SLAERGIDPN
VVDDQRGRLT FASEIARAIA HLLRTRAPYG TYNVSGSGEP RTWAELAGDI FALTGADRAR
VSGVSTETYF AGATGPVAPR PLNSVLDLSK LEATGFAPRD AGEQLKEYLA S
//
