ID H5USD8_9MICO Unreviewed; 460 AA.
AC H5USD8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN Name=rmlC {ECO:0000313|EMBL:GAB48646.1};
GN Synonyms=rmlD {ECO:0000313|EMBL:GAB48646.1};
GN ORFNames=MOPEL_078_00350 {ECO:0000313|EMBL:GAB48646.1};
OS Mobilicoccus pelagius NBRC 104925.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC Mobilicoccus.
OX NCBI_TaxID=1089455 {ECO:0000313|EMBL:GAB48646.1, ECO:0000313|Proteomes:UP000004367};
RN [1] {ECO:0000313|EMBL:GAB48646.1, ECO:0000313|Proteomes:UP000004367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 104925 {ECO:0000313|EMBL:GAB48646.1,
RC ECO:0000313|Proteomes:UP000004367};
RA Yoshida Y., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Mobilicoccus pelagius NBRC 104925.";
RL Submitted (FEB-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 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:GAB48646.1}.
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DR EMBL; BAFE01000056; GAB48646.1; -; Genomic_DNA.
DR RefSeq; WP_009482544.1; NZ_BAFE01000056.1.
DR AlphaFoldDB; H5USD8; -.
DR STRING; 1089455.MOPEL_078_00350; -.
DR eggNOG; COG1091; Bacteria.
DR eggNOG; COG1898; Bacteria.
DR OrthoDB; 9803892at2; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000004367; 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:UP000004367}.
FT DOMAIN 188..459
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
FT ACT_SITE 66
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600888-1"
FT ACT_SITE 129
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600888-1"
FT SITE 135
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 460 AA; 49189 MW; F8F785A935949CA6 CRC64;
MTDLAVHTTD IPGLLVVDLP VHGDNRGWFK ENWQRAKMTG LGLPDFGPVQ QNVSFNDEVG
VTRGVHAEPW DKFVSVATGR VFGAWVDLRA GDTFGAVVTC EITPERAVFV PRGVGNAYQT
LEPATAYSYL VNDHWSPAAK ERYTFVQLGD PELAIPWPIP LEKAILSDAD KAHPALADAT
PFTPGRAVVL GASGQLGRAL RGALPDAVFL TRAEADLTEP ASLSGIDLDG IDTIVNAAAY
TAVDAAETPE GRREAWAANV AGVGALVDLA RRHSCRLVHV SSDYVFDGTA EEHDEDEPFS
PLGVYGQTKA AGDALVASWG KHYIVRTSWV VGEGRNFVAT MAALADKGVS PSVVDDQYGR
LTFTQDLAAG IAHLLAAGAE YGTYNLTNSG PVQTWADIAA DVYELRGRSR DDVTRVSTEE
YGAGKDMAPR PTHSALDLAK ITAAGFDVPH ASERLRRMLA
//
