RMLB_MYCS2
ID RMLB_MYCS2 Reviewed; 331 AA.
AC A0QSK6; I7G5T4;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=MSMEG_1512, MSMEI_1476;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION IN DTDP-RHAMNOSE BIOSYNTHESIS, AND PATHWAY.
RX PubMed=16472764; DOI=10.1016/j.bbrc.2006.01.130;
RA Li W., Xin Y., McNeil M.R., Ma Y.;
RT "rmlB and rmlC genes are essential for growth of mycobacteria.";
RL Biochem. Biophys. Res. Commun. 342:170-178(2006).
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 (By similarity). Involved in the biosynthesis
CC of the dTDP-L-rhamnose which is a component of the critical linker, D-
CC N-acetylglucosamine-L-rhamnose disaccharide, which connects the
CC galactan region of arabinogalactan to peptidoglycan via a
CC phosphodiester linkage (PubMed:16472764).
CC {ECO:0000250|UniProtKB:P27830, ECO:0000269|PubMed:16472764}.
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:0000305|PubMed:16472764}.
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; CP000480; ABK70086.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP37949.1; -; Genomic_DNA.
DR RefSeq; WP_003892900.1; NZ_SIJM01000016.1.
DR RefSeq; YP_885894.1; NC_008596.1.
DR AlphaFoldDB; A0QSK6; -.
DR SMR; A0QSK6; -.
DR STRING; 246196.MSMEI_1476; -.
DR EnsemblBacteria; ABK70086; ABK70086; MSMEG_1512.
DR EnsemblBacteria; AFP37949; AFP37949; MSMEI_1476.
DR GeneID; 66732969; -.
DR KEGG; msg:MSMEI_1476; -.
DR KEGG; msm:MSMEG_1512; -.
DR PATRIC; fig|246196.19.peg.1497; -.
DR eggNOG; COG1088; Bacteria.
DR OMA; KLIPLMC; -.
DR OrthoDB; 707977at2; -.
DR UniPathway; UPA00124; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; IGI:UniProtKB.
DR GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IGI:UniProtKB.
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 1: Evidence at protein level;
KW Lyase; NAD; Reference proteome.
FT CHAIN 1..331
FT /note="dTDP-glucose 4,6-dehydratase"
FT /id="PRO_0000399898"
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; 36967 MW; 7DC0A0520677DDF0 CRC64;
MRLLVTGGAG FIGANFVHLA LREARTSSIT VLDALTYAGS RESLAPVADR IRLVQGDITD
AALVGDLVAE SDAVVHFAAE THVDNALADP EPFLHSNVVG TYTILEAVRR HNVRLHHVST
DEVYGDLELD NPARFNETTP YNPSSPYSST KAAADLLVRA WVRSYGVRAT ISNCSNNYGP
YQHVEKFIPR QITNVLTGRR PKLYGAGANV RDWIHVDDHN SAVWRILTDG TIGRTYLIGA
ECERNNLTVM RTILKLMGRD PDDFDHVTDR AGHDLRYAID PSTLQDELGW APKHTDFEAG
LTDTIDWYRA NESWWRPLKD TVEAKYQERG Q
