ID A0A1Y4ASH9_9ACTN Unreviewed; 495 AA.
AC A0A1Y4ASH9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000256|RuleBase:RU364082};
DE EC=1.1.1.133 {ECO:0000256|RuleBase:RU364082};
GN ORFNames=B5F89_02980 {ECO:0000313|EMBL:OUO21821.1};
OS Collinsella sp. An307.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC Coriobacteriaceae; Collinsella.
OX NCBI_TaxID=1965630 {ECO:0000313|EMBL:OUO21821.1, ECO:0000313|Proteomes:UP000196349};
RN [1] {ECO:0000313|Proteomes:UP000196349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An307 {ECO:0000313|Proteomes:UP000196349};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUO21821.1}.
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DR EMBL; NFIP01000002; OUO21821.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4ASH9; -.
DR OrthoDB; 9803892at2; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000196349; 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:UP000196349}.
FT DOMAIN 194..493
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
FT ACT_SITE 73
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600888-1"
FT ACT_SITE 137
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600888-1"
FT SITE 143
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 495 AA; 53631 MW; CD054A738E0685D4 CRC64;
MADIAYEKEL GLTETGIPGL VVVDLAVHGD NRGWFKENWQ RAKMALGLGL PDRRWVQNNI
SFNTQRGATR GIHAEPWDKF ISVATGSVFG AWVDLRAGSP AYGRVFTCTL DPSRAIYVPR
GVGNSYQALE DGTAYTYLVD AHWSAELKGT YTFVNLADPE LAIDWPIPLA EAELSDADRA
HPLLRDVRPM EPRRTLVTGA NGQLGRAVRA LAEERGLMAF DYCDIDTFDM SDPAAYGTVD
WDLYGTVINC GAYTAVDAAE TPEGRVTCWK ANATGPALLA RTCAERGISL VHVSSDYVFD
GTRELHTEDE PLSPLGVYGQ SKAAGDLAVA GCPAHWIVRS SWVIGDGRNF VKTMCALSDR
VADAGDALLE VTVVDDQVGR LTFTRDMAEG ILWLLGYREG SVLPAASAPC GTYNLTGEGR
AASWADIARE VFELANGNGG AVRPVTTAEY YAKATGPVSP RPEHSALDLA KIEAAGFTPR
DWEEELCDYV RALRA
//
