Tag | Content |
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CPLM ID | CPLM-006793 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | dTDP-glucose 4,6-dehydratase 1 |
Protein Synonyms/Alias | |
Gene Name | rfbB |
Gene Synonyms/Alias | rmlB; b2041; JW2026 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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33 | DSVVNVDKLTYAGNR | acetylation | [1] | 122 | WSALDSDKKNSFRFH | acetylation | [1] | 226 | KALPIYGKGDQIRDW | acetylation | [1] | 251 | YTVVTEGKAGETYNI | acetylation | [1] | 310 | RYAIDAEKIGRALGW | acetylation | [1] | 318 | IGRALGWKPQETFES | acetylation | [1] | 339 | EWYLSNTKWVDNVKS | acetylation | [1] |
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Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Catalyzes the dehydration of dTDP-D-glucose to form dTDP-6-deoxy-D-xylo-4-hexulose via a three-step process involving oxidation, dehydration and reduction (By similarity). |
Sequence Annotation | NP_BIND 7 13 NAD (Potential). NP_BIND 32 35 NAD (By similarity). NP_BIND 58 59 NAD (By similarity). NP_BIND 167 171 NAD (By similarity). REGION 133 135 Substrate binding (By similarity). REGION 206 207 Substrate binding (By similarity). REGION 222 224 Substrate binding (By similarity). REGION 297 300 Substrate binding (By similarity). ACT_SITE 134 134 Proton donor (By similarity). ACT_SITE 135 135 Proton acceptor (By similarity). ACT_SITE 167 167 Proton acceptor (By similarity). BINDING 80 80 NAD; via carbonyl oxygen (By similarity). BINDING 84 84 Substrate; via carbonyl oxygen (By BINDING 99 99 NAD (By similarity). BINDING 196 196 Substrate (By similarity). BINDING 197 197 NAD; via amide nitrogen (By similarity). BINDING 231 231 Substrate (By similarity). BINDING 266 266 Substrate (By similarity). BINDING 357 357 Substrate (By similarity). |
Keyword | Complete proteome; Lipopolysaccharide biosynthesis; Lyase; NAD; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 361 AA |
Protein Sequence | MKILVTGGAG FIGSAVVRHI INNTQDSVVN VDKLTYAGNR ESLADVSDSE RYVFEHADIC 60 DAPAMARIFA QHQPDAVMHL AAESHVDRSI TGPAAFIETN IVGTYVLLEA ARNYWSALDS 120 DKKNSFRFHH ISTDEVYGDL PHPDEVNNTE ELPLFTETTA YAPSSPYSAS KASSDHLVRA 180 WKRTYGLPTI VTNCSNNYGP YHFPEKLIPL VILNALEGKA LPIYGKGDQI RDWLYVEDHA 240 RALYTVVTEG KAGETYNIGG HNEKKNIDVV LTICDLLDEI VPKEKSYREQ ITYVADRPGH 300 DRRYAIDAEK IGRALGWKPQ ETFESGIRKT VEWYLSNTKW VDNVKSGAYQ SWIEQNYEGR 360 Q 361 |
Gene Ontology | GO:0050662; F:coenzyme binding; IEA:InterPro. GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; ISS:UniProtKB. GO:0019305; P:dTDP-rhamnose biosynthetic process; IEA:UniProtKB-UniPathway. GO:0045226; P:extracellular polysaccharide biosynthetic process; ISS:UniProtKB. GO:0009103; P:lipopolysaccharide biosynthetic process; ISS:UniProtKB. GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |