ID A0A3M9N5G1_9BACT Unreviewed; 748 AA.
AC A0A3M9N5G1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN Name=rfbD {ECO:0000313|EMBL:RNI33044.1};
GN ORFNames=EFA69_01070 {ECO:0000313|EMBL:RNI33044.1};
OS Rufibacter immobilis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Rufibacter.
OX NCBI_TaxID=1348778 {ECO:0000313|EMBL:RNI33044.1, ECO:0000313|Proteomes:UP000271010};
RN [1] {ECO:0000313|EMBL:RNI33044.1, ECO:0000313|Proteomes:UP000271010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCC P1 {ECO:0000313|EMBL:RNI33044.1,
RC ECO:0000313|Proteomes:UP000271010};
RA Yang Y.;
RT "Rufibacter latericius sp. nov., isolated from water in Baiyang Lake.";
RL Submitted (NOV-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 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:RNI33044.1}.
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DR EMBL; RJJE01000001; RNI33044.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M9N5G1; -.
DR OrthoDB; 9803892at2; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000271010; Unassembled WGS sequence.
DR GO; GO:0008831; F:dTDP-4-dehydrorhamnose reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05254; dTDP_HR_like_SDR_e; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 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; IPR001360; Glyco_hydro_1.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
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; PF00232; Glyco_hydro_1; 1.
DR Pfam; PF04321; RmlD_sub_bind; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 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,
KW ECO:0000313|EMBL:RNI33044.1}.
FT DOMAIN 449..705
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 748 AA; 84048 MW; 03BBFA1B0CF570BA CRC64;
MANIELWGGV ECTVNRVGEQ YFDQLAQSGH ARRLSDLDLF AELGIKKIRY PVLWESVAPD
HPEQKNWDWA TERLNRLREL TIEPIVGLLH HGSGPRYTHL IDEDFPHKFA QYARAVARQF
PWVTYYTPIN EPLTTARFSA LYGLWYPHTR DDASFVKALL NQIQGTKLAM EAIREINPSA
QLVQTDDLGY SHSTPALQYQ ADFENHRRWL TWDLLCGKVN QQHPLWNYLL KAKAPETLLL
ELLENPCPPN VIGVNYYVTS ERYLDEHIAD YPWHTHGSNQ KHRYADVEAV RVQAASPLGA
QKILEQACDR YNLPVAITEA HLCCTREEQM RWFTEVWDAA SLLKEQGKNV LGVTAWTLLG
AYDWNSLLTQ NRGHYEMGVY DLRGGEPART AVSELLTGIA SGAERHPLLQ VPGWWNRACR
SVYPPSAECP EVWDISLNKS KQGSKLQPLL ITGATGTLGR AFARVCDIRG IPYVLLSRQQ
MDITNEDSVR KALTQYKPWA VVNTAGYVRV DQAEQEPEAC FRENTLGPAV LAKICQEEQV
QLVTFSSDLV FGGEKMVVYT EQDTPQPLNV YGRSKAEAEA QVLAAMPTAL VIRTSAFFGP
WDEHNFVYHA LKAMVRQEPL EAAADQFITP TYVPDLVNTT LDLLIDAESG IWHLANRGTY
SWAEFAALAA NMAGLDPKPW LEAVPSAKIG QPAARPMFSG LGTVKRGVLP TVEDALQRFL
HATQFPVRPS LPPQEEEVAD QSLLSAGA
//
