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RMLB_MYCTU
ID   RMLB_MYCTU              Reviewed;         331 AA.
AC   P9WN65; 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 43.
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=Rv3464;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   FUNCTION IN DTDP-RHAMNOSE BIOSYNTHESIS, AND PATHWAY.
RC   STRAIN=ATCC 25618 / H37Rv;
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).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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; AL123456; CCP46286.1; -; Genomic_DNA.
DR   PIR; E70566; E70566.
DR   RefSeq; NP_217981.1; NC_000962.3.
DR   RefSeq; WP_003418607.1; NZ_NVQJ01000091.1.
DR   AlphaFoldDB; P9WN65; -.
DR   SMR; P9WN65; -.
DR   STRING; 83332.Rv3464; -.
DR   PaxDb; P9WN65; -.
DR   DNASU; 887332; -.
DR   GeneID; 887332; -.
DR   KEGG; mtu:Rv3464; -.
DR   TubercuList; Rv3464; -.
DR   eggNOG; COG1088; Bacteria.
DR   OMA; KLIPLMC; -.
DR   PhylomeDB; P9WN65; -.
DR   BRENDA; 4.2.1.46; 3445.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR   GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; IDA:MTBBASE.
DR   GO; GO:0070404; F:NADH binding; ISS:UniProtKB.
DR   GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IDA:MTBBASE.
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_0000395348"
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
 
 
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