ID U1MWF3_9MICO Unreviewed; 472 AA.
AC U1MWF3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, 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=L332_10855 {ECO:0000313|EMBL:ERG64940.1};
OS Agrococcus pavilionensis RW1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agrococcus.
OX NCBI_TaxID=1330458 {ECO:0000313|EMBL:ERG64940.1, ECO:0000313|Proteomes:UP000016462};
RN [1] {ECO:0000313|EMBL:ERG64940.1, ECO:0000313|Proteomes:UP000016462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RW1 {ECO:0000313|EMBL:ERG64940.1,
RC ECO:0000313|Proteomes:UP000016462};
RX PubMed=23814108;
RA White R.A.III., Grassa C.J., Suttle C.A.;
RT "First draft genome sequence from a member of the genus agrococcus,
RT isolated from modern microbialites.";
RL Genome Announc. 1:e00391-13(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:ERG64940.1}.
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DR EMBL; ASHR01000014; ERG64940.1; -; Genomic_DNA.
DR RefSeq; WP_021009959.1; NZ_ASHR01000014.1.
DR AlphaFoldDB; U1MWF3; -.
DR OrthoDB; 9803892at2; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000016462; 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 NADP {ECO:0000256|RuleBase:RU364082};
KW Oxidoreductase {ECO:0000256|RuleBase:RU364082};
KW Reference proteome {ECO:0000313|Proteomes:UP000016462}.
FT DOMAIN 192..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 472 AA; 51183 MW; 3254D0762CD3D68B CRC64;
MADVATGKPL RIRETPIPGF LVVDLPVHGD NRGWFKENWQ REKMLALGLP DFGPVQNNIS
FNAAPGVTRG IHAEPWDKYI SVASGRVFGA WVDLREGDSF GATFTIEIDP SIAVFVPRGV
GNAFQALEVD TAYSYLVNDH WSADAQDEYT FLNLADPTAA IEWPIPLADA ELSDKDRAHP
MLGDVEPMRP RRTLVLGASG QLGRALRQQW AGRADVDYVG RDTVDLADPS TLDAVRWSHY
DTVVNAAAHT AVDGAETAEG RRDAWAANAS GPARLAAIAA EHRLTLVHVS SDYVFDGTVP
EHDEAERFAP LGVYGQSKAA GDLAVSVAPR HYILRTSWVV GEGKNFIATM ASLAERGIDP
AVVGDQVGRL TFASELARAI DHLLATRAPF GTYNVSNGGE PASWADIAAR VFERTGHDAS
RVTPVTTEEY YAGKEGIAPR PLQSTLSLAR LESTGFEPRD QLEMLDAFVR SL
//
