ID A0A2T0V3B5_9MICO Unreviewed; 468 AA.
AC A0A2T0V3B5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN ORFNames=B0I08_11236 {ECO:0000313|EMBL:PRY64651.1};
OS Glaciihabitans tibetensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Glaciihabitans.
OX NCBI_TaxID=1266600 {ECO:0000313|EMBL:PRY64651.1, ECO:0000313|Proteomes:UP000237983};
RN [1] {ECO:0000313|EMBL:PRY64651.1, ECO:0000313|Proteomes:UP000237983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12484 {ECO:0000313|EMBL:PRY64651.1,
RC ECO:0000313|Proteomes:UP000237983};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAR-2018) 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:PRY64651.1}.
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DR EMBL; PVTL01000012; PRY64651.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0V3B5; -.
DR OrthoDB; 9803892at2; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000237983; 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 NADP {ECO:0000256|RuleBase:RU364082};
KW Oxidoreductase {ECO:0000256|RuleBase:RU364082};
KW Reference proteome {ECO:0000313|Proteomes:UP000237983}.
FT DOMAIN 190..465
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
FT ACT_SITE 70
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600888-1"
FT ACT_SITE 133
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600888-1"
FT SITE 139
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 468 AA; 50856 MW; 09D9DCB5500BAF97 CRC64;
MVQVGKTLEA TSTPIPGLLV IELPVHGDNR GWFKENWQRE KMLALGLPDF GPVQNNISFN
TEVGTTRGIH AEPWDKYVSV ATGKIFGAWV DLREGPSFGA VFTAELDASK AIFVPRGVGN
SFQTLEPDTA YSYLVNDHWS ADAQTRYTFL NLADETAAIA WPISLVDAAL SDKDRAHPRL
ADVTPMPAKK TLILGANGQV GRALVSILPN ARAVDRSEFD ITDAAAYETF DWGSYDTIIN
AAAYTAVDVA ETPDGRRACW EINVTATALL ARVATANRMT LVHISSDYVF DGTTEVHTEE
EQLSPLGVYG QSKAAADAIV STVPDHYIVR TSWVIGDGNN FVRTMASLAA RDVSPTVVND
QYGRLSFADD IAAGIVHLLA ARPESGVYNL SNDGPSHSWA EIAQQIFELV GKDPSQVAGV
STTEYFSERS AAPRPTHSVL NLTKLEVVGF RPREAREALR NYLRSSTP
//
