Tag | Content |
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CPLM ID | CPLM-010317 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Bifunctional polymyxin resistance protein ArnA |
Protein Synonyms/Alias | Polymyxin resistance protein PmrI; UDP-4-amino-4-deoxy-L-arabinose formyltransferase; ArnAFT; UDP-L-Ara4N formyltransferase; UDP-glucuronic acid oxidase, UDP-4-keto-hexauronic acid decarboxylating; ArnADH; UDP-GlcUA decarboxylase; UDP-glucuronic acid dehydrogenase |
Gene Name | arnA |
Gene Synonyms/Alias | pmrI; yfbG; b2255; JW2249 |
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 | IAITLHHKLCHAARQ | acetylation | [1] | 181 | EQTLPAIKHGNILEI | acetylation | [1] | 212 | DSFLEWHKPASVLHN | acetylation | [1] | 442 | VYGMCSDKYFDEDHS | acetylation | [1] | 458 | LIVGPVNKPRWIYSV | acetylation | [1] | 526 | LVEGSPIKLIDGGKQ | acetylation | [1] | 611 | ESSSYYGKGYQDVEH | 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 | Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto- arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4- amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido- arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. |
Sequence Annotation | NP_BIND 368 369 NAD binding. REGION 1 304 Formyltransferase ArnAFT. REGION 86 88 10-formyltetrahydrofolate binding. REGION 136 140 10-formyltetrahydrofolate binding. REGION 314 660 Dehydrogenase ArnADH. REGION 432 433 UDP-glucuronate binding. REGION 526 535 UDP-glucuronate binding. ACT_SITE 104 104 Proton donor; for formyltransferase ACT_SITE 434 434 Proton acceptor; for decarboxylase ACT_SITE 619 619 Proton donor; for decarboxylase activity. BINDING 114 114 10-formyltetrahydrofolate. BINDING 347 347 NAD. BINDING 393 393 UDP-glucuronate; via carbonyl oxygen. BINDING 398 398 UDP-glucuronate. BINDING 460 460 UDP-glucuronate. BINDING 492 492 UDP-glucuronate. BINDING 613 613 UDP-glucuronate. |
Keyword | 3D-structure; Antibiotic resistance; Complete proteome; Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism; Lipopolysaccharide biosynthesis; Multifunctional enzyme; NAD; Oxidoreductase; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 660 AA |
Protein Sequence | MKTVVFAYHD MGCLGIEALL AAGYEISAIF THTDNPGEKA FYGSVARLAA ERGIPVYAPD 60 NVNHPLWVER IAQLSPDVIF SFYYRHLIYD EILQLAPAGA FNLHGSLLPK YRGRAPLNWV 120 LVNGETETGV TLHRMVKRAD AGAIVAQLRI AIAPDDIAIT LHHKLCHAAR QLLEQTLPAI 180 KHGNILEIAQ RENEATCFGR RTPDDSFLEW HKPASVLHNM VRAVADPWPG AFSYVGNQKF 240 TVWSSRVHPH ASKAQPGSVI SVAPLLIACG DGALEIVTGQ AGDGITMQGS QLAQTLGLVQ 300 GSRLNSQPAC TARRRTRVLI LGVNGFIGNH LTERLLREDH YEVYGLDIGS DAISRFLNHP 360 HFHFVEGDIS IHSEWIEYHV KKCDVVLPLV AIATPIEYTR NPLRVFELDF EENLRIIRYC 420 VKYRKRIIFP STSEVYGMCS DKYFDEDHSN LIVGPVNKPR WIYSVSKQLL DRVIWAYGEK 480 EGLQFTLFRP FNWMGPRLDN LNAARIGSSR AITQLILNLV EGSPIKLIDG GKQKRCFTDI 540 RDGIEALYRI IENAGNRCDG EIINIGNPEN EASIEELGEM LLASFEKHPL RHHFPPFAGF 600 RVVESSSYYG KGYQDVEHRK PSIRNAHRCL DWEPKIDMQE TIDETLDFFL RTVDLTDKPS 660 |
Gene Ontology | GO:0050662; F:coenzyme binding; IEA:InterPro. GO:0016742; F:hydroxymethyl-, formyl- and related transferase activity; IDA:EcoCyc. GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:EcoCyc. GO:0009245; P:lipid A biosynthetic process; IDA:EcoCyc. GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway. GO:0046677; P:response to antibiotic; IDA:EcoCyc. |
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