RMLB_MYCTO
ID RMLB_MYCTO Reviewed; 331 AA.
AC P9WN64; L0TFH5; O06329; Q7D5I4;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=dTDP-glucose 4,6-dehydratase {ECO:0000250|UniProtKB:P27830};
DE EC=4.2.1.46 {ECO:0000250|UniProtKB:P27830};
GN Name=rmlB; Synonyms=rfbB; OrderedLocusNames=MT3570;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Catalyzes the dehydration of dTDP-D-glucose to form dTDP-6-
CC deoxy-D-xylo-4-hexulose via a three-step process involving oxidation,
CC dehydration and reduction. Involved in the biosynthesis of the dTDP-L-
CC rhamnose which is a component of the critical linker, D-N-
CC acetylglucosamine-L-rhamnose disaccharide, which connects the galactan
CC region of arabinogalactan to peptidoglycan via a phosphodiester
CC linkage. {ECO:0000250|UniProtKB:P27830, ECO:0000250|UniProtKB:P9WN65}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose
CC + H2O; Xref=Rhea:RHEA:17221, ChEBI:CHEBI:15377, ChEBI:CHEBI:57477,
CC ChEBI:CHEBI:57649; EC=4.2.1.46;
CC Evidence={ECO:0000250|UniProtKB:P27830};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000250|UniProtKB:P27830};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000250|UniProtKB:P27830};
CC -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC {ECO:0000250|UniProtKB:P9WN65}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P27830}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. dTDP-glucose dehydratase subfamily. {ECO:0000305}.
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DR EMBL; AE000516; AAK47910.1; -; Genomic_DNA.
DR PIR; E70566; E70566.
DR RefSeq; WP_003418607.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WN64; -.
DR SMR; P9WN64; -.
DR EnsemblBacteria; AAK47910; AAK47910; MT3570.
DR KEGG; mtc:MT3570; -.
DR PATRIC; fig|83331.31.peg.3827; -.
DR HOGENOM; CLU_007383_1_14_11; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05246; dTDP_GD_SDR_e; 1.
DR InterPro; IPR005888; dTDP_Gluc_deHydtase.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01181; dTDP_gluc_dehyt; 1.
PE 3: Inferred from homology;
KW Lyase; NAD.
FT CHAIN 1..331
FT /note="dTDP-glucose 4,6-dehydratase"
FT /id="PRO_0000427181"
FT ACT_SITE 121
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT ACT_SITE 122
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 11..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 33..36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 57..58
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 77..81
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 96
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 147..151
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 177
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 186..191
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P95780"
FT BINDING 202..204
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P95780"
FT BINDING 211
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 269..273
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
SQ SEQUENCE 331 AA; 37558 MW; 10652C75423082D2 CRC64;
MRLLVTGGAG FIGTNFVHSA VREHPDDAVT VLDALTYAGR RESLADVEDA IRLVQGDITD
AELVSQLVAE SDAVVHFAAE SHVDNALDNP EPFLHTNVIG TFTILEAVRR HGVRLHHIST
DEVYGDLELD DRARFTESTP YNPSSPYSAT KAGADMLVRA WVRSYGVRAT ISNCSNNYGP
YQHVEKFIPR QITNVLTGRR PKLYGAGANV RDWIHVDDHN SAVRRILDRG RIGRTYLISS
EGERDNLTVL RTLLRLMDRD PDDFDHVTDR VGHDLRYAID PSTLYDELCW APKHTDFEEG
LRTTIDWYRD NESWWRPLKD ATEARYQERG Q
