Tag | Content |
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CPLM ID | CPLM-010346 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase |
Protein Synonyms/Alias | Polymyxin resistance protein PmrH; UDP-(beta-L-threo-pentapyranosyl-4''-ulose diphosphate) aminotransferase; UDP-Ara4O aminotransferase; UDP-4-amino-4-deoxy-L-arabinose aminotransferase |
Gene Name | arnB |
Gene Synonyms/Alias | pmrH; yfbE; b2253; JW5372 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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164 | HAVGTYYKGRHIGAK | acetylation | [1] | 207 | ARQLRMLKFHGLGVD | acetylation | [1] | 235 | EVLTPGYKYNLTDIN | acetylation | [1] | 314 | DALMEALKERGIGTG | acetylation | [1] | 331 | FRAAHTQKYYRERFP | 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 conversion of UDP-4-keto-arabinose (UDP- Ara4O) to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. |
Sequence Annotation | MOD_RES 182 182 N6-(pyridoxal phosphate)lysine (By |
Keyword | Aminotransferase; Antibiotic resistance; Complete proteome; Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism; Lipopolysaccharide biosynthesis; Pyridoxal phosphate; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 379 AA |
Protein Sequence | MSEFLPFSRP AMGVEELAAV KEVLESGWIT TGPKNQALEQ AFCQLTGNQH AIAVSSATAG 60 MHITLMALKI GKGDEVITPS LTWVSTLNMI SLLGATPVMV DVDRDTLMVT PEAIESAITP 120 RTKAIIPVHY AGAPADIDAI RAIGERYGIA VIEDAAHAVG TYYKGRHIGA KGTAIFSFHA 180 IKNITCAEGG LIVTDNENLA RQLRMLKFHG LGVDAYDRQT WGRAPQAEVL TPGYKYNLTD 240 INAAIALTQL VKLEHLNTRR REIAQQYQQA LAALPFQPLS LPAWPHVHAW HLFIIRVDEQ 300 RCGISRDALM EALKERGIGT GLHFRAAHTQ KYYRERFPTL SLPNTEWNSE RICSLPLFPD 360 MTTADADHVI TALQQLAGQ 379 |
Gene Ontology | GO:0005737; C:cytoplasm; NAS:EcoCyc. GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc. GO:0008483; F:transaminase activity; IDA:EcoCyc. GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-KW. GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway. GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. |
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