CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
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
164IAITLHHKLCHAARQacetylation[1]
181EQTLPAIKHGNILEIacetylation[1]
212DSFLEWHKPASVLHNacetylation[1]
442VYGMCSDKYFDEDHSacetylation[1]
458LIVGPVNKPRWIYSVacetylation[1]
526LVEGSPIKLIDGGKQacetylation[1]
611ESSSYYGKGYQDVEHacetylation[1]
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. 
Interpro
 IPR021168; Bifun_polymyxin_resist_ArnA.
 IPR001509; Epimerase_deHydtase.
 IPR005793; Formyl_trans_C.
 IPR002376; Formyl_transf_N.
 IPR011034; Formyl_transferase_C-like.
 IPR016040; NAD(P)-bd_dom. 
Pfam
 PF01370; Epimerase
 PF02911; Formyl_trans_C
 PF00551; Formyl_trans_N 
SMART
  
PROSITE
  
PRINTS