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RMLC_MYCS2
ID   RMLC_MYCS2              Reviewed;         201 AA.
AC   A0QSK5; I7FGH4;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=dTDP-4-dehydrorhamnose 3,5-epimerase {ECO:0000305};
DE            EC=5.1.3.13 {ECO:0000269|PubMed:16472764};
DE   AltName: Full=Thymidine diphospho-4-keto-rhamnose 3,5-epimerase {ECO:0000305};
DE   AltName: Full=dTDP-4-keto-6-deoxyglucose 3,5-epimerase {ECO:0000305};
DE   AltName: Full=dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase {ECO:0000305};
DE   AltName: Full=dTDP-L-rhamnose synthase {ECO:0000305};
GN   Name=rmlC; OrderedLocusNames=MSMEG_1510, MSMEI_1475;
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 CATALYTIC ACTIVITY.
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 epimerization of the C3' and C5'positions of
CC       dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
CC       Involved in the biosynthesis of the dTDP-L-rhamnose which is a
CC       component of the critical linker, D-N-acetylglucosamine-L-rhamnose
CC       disaccharide, which connects the galactan region of arabinogalactan to
CC       peptidoglycan via a phosphodiester linkage.
CC       {ECO:0000269|PubMed:16472764}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-
CC         L-rhamnose; Xref=Rhea:RHEA:16969, ChEBI:CHEBI:57649,
CC         ChEBI:CHEBI:62830; EC=5.1.3.13;
CC         Evidence={ECO:0000269|PubMed:16472764};
CC   -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC       {ECO:0000250|UniProtKB:P26394}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WH11}.
CC   -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000480; ABK71239.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP37948.1; -; Genomic_DNA.
DR   RefSeq; WP_011727714.1; NZ_SIJM01000016.1.
DR   RefSeq; YP_885893.1; NC_008596.1.
DR   AlphaFoldDB; A0QSK5; -.
DR   SMR; A0QSK5; -.
DR   STRING; 246196.MSMEI_1475; -.
DR   EnsemblBacteria; ABK71239; ABK71239; MSMEG_1510.
DR   EnsemblBacteria; AFP37948; AFP37948; MSMEI_1475.
DR   GeneID; 66732968; -.
DR   KEGG; msg:MSMEI_1475; -.
DR   KEGG; msm:MSMEG_1510; -.
DR   PATRIC; fig|246196.19.peg.1496; -.
DR   eggNOG; COG1898; Bacteria.
DR   OMA; RGVFLEW; -.
DR   OrthoDB; 1618609at2; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
DR   GO; GO:0008830; F:dTDP-4-dehydrorhamnose 3,5-epimerase 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   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR000888; dTDP_sugar_isom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   PANTHER; PTHR21047; PTHR21047; 1.
DR   Pfam; PF00908; dTDP_sugar_isom; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Isomerase; Reference proteome.
FT   CHAIN           1..201
FT                   /note="dTDP-4-dehydrorhamnose 3,5-epimerase"
FT                   /id="PRO_0000399899"
FT   ACT_SITE        62
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   ACT_SITE        132
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         23
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         28
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         47..49
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         59
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   SITE            138
FT                   /note="Participates in a stacking interaction with the
FT                   thymidine ring of dTDP-4-oxo-6-deoxyglucose"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SFD1"
SQ   SEQUENCE   201 AA;  22241 MW;  7E3E273F547CBE7F CRC64;
     MTARELSIAG AWEITPVLRT DSRGLFFEWF TDAGFTEFAG HQFDMRQANC SVSARGVLRG
     VHFAQVPPSQ AKYVTCVRGA VFDVVVDIRV GSPTFGQWDA VLLDDKDRRS IYISEGLGHA
     FLALDDDSTV MYLCSAPYAP QREHTVRPTD FGIEWPEVPE LILSDRDAQA PSLAEAQAAG
     VLPTWADCQA FVETLRRNLV S
 
 
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