ID ARND_ECO24 Reviewed; 296 AA. AC A7ZP74; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 27-MAR-2024, entry version 83. DE RecName: Full=Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD {ECO:0000255|HAMAP-Rule:MF_01870}; DE EC=3.5.1.n3 {ECO:0000255|HAMAP-Rule:MF_01870}; GN Name=arnD {ECO:0000255|HAMAP-Rule:MF_01870}; GN OrderedLocusNames=EcE24377A_2551; OS Escherichia coli O139:H28 (strain E24377A / ETEC). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=331111; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E24377A / ETEC; RX PubMed=18676672; DOI=10.1128/jb.00619-08; RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., RA Henderson I.R., Sperandio V., Ravel J.; RT "The pangenome structure of Escherichia coli: comparative genomic analysis RT of E. coli commensal and pathogenic isolates."; RL J. Bacteriol. 190:6881-6893(2008). CC -!- FUNCTION: Catalyzes the deformylation of 4-deoxy-4-formamido-L- CC arabinose-phosphoundecaprenol to 4-amino-4-deoxy-L-arabinose- CC phosphoundecaprenol. The modified arabinose is attached to lipid A and CC is required for resistance to polymyxin and cationic antimicrobial CC peptides. {ECO:0000255|HAMAP-Rule:MF_01870}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4-deoxy-4-formamido-alpha-L-arabinopyranosyl di-trans,octa- CC cis-undecaprenyl phosphate + H2O = 4-amino-4-deoxy-alpha-L- CC arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + formate; CC Xref=Rhea:RHEA:27734, ChEBI:CHEBI:15377, ChEBI:CHEBI:15740, CC ChEBI:CHEBI:58909, ChEBI:CHEBI:60463; EC=3.5.1.n3; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01870}; CC -!- PATHWAY: Glycolipid biosynthesis; 4-amino-4-deoxy-alpha-L-arabinose CC undecaprenyl phosphate biosynthesis; 4-amino-4-deoxy-alpha-L-arabinose CC undecaprenyl phosphate from UDP-4-deoxy-4-formamido-beta-L-arabinose CC and undecaprenyl phosphate: step 2/2. {ECO:0000255|HAMAP- CC Rule:MF_01870}. CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01870}. CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family. ArnD CC deformylase subfamily. {ECO:0000255|HAMAP-Rule:MF_01870}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000800; ABV17216.1; -; Genomic_DNA. DR RefSeq; WP_000169738.1; NC_009801.1. DR AlphaFoldDB; A7ZP74; -. DR SMR; A7ZP74; -. DR GeneID; 66673858; -. DR KEGG; ecw:EcE24377A_2551; -. DR HOGENOM; CLU_084199_0_0_6; -. DR UniPathway; UPA00030; -. DR UniPathway; UPA00036; UER00496. DR Proteomes; UP000001122; Chromosome. DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:UniProtKB-UniRule. DR GO; GO:0036108; P:4-amino-4-deoxy-alpha-L-arabinopyranosyl undecaprenyl phosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR CDD; cd10939; CE4_ArnD; 1. DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1. DR HAMAP; MF_01870; ArnD; 1. DR InterPro; IPR023557; ArnD. DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl. DR InterPro; IPR002509; NODB_dom. DR PANTHER; PTHR10587:SF105; CHITIN DEACETYLASE 1-RELATED; 1. DR PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-RELATED; 1. DR Pfam; PF01522; Polysacc_deac_1; 1. DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1. DR PROSITE; PS51677; NODB; 1. PE 3: Inferred from homology; KW Antibiotic resistance; Hydrolase; Lipid A biosynthesis; Lipid biosynthesis; KW Lipid metabolism; Lipopolysaccharide biosynthesis; Reference proteome. FT CHAIN 1..296 FT /note="Probable 4-deoxy-4-formamido-L-arabinose- FT phosphoundecaprenol deformylase ArnD" FT /id="PRO_0000383502" FT DOMAIN 2..260 FT /note="NodB homology" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01870" SQ SEQUENCE 296 AA; 33142 MW; 7DC4B1938195D14A CRC64; MTKVGLRIDV DTFRGTREGV PRLLEILSKH NIQASIFFSV GPDNMGRHLW RLVKPQFLWK MLRSNAASLY GWDILLAGTA WPGKEIGHAN ADIIREAAKH HEVGLHAWDH HAWQARSSNW DRQTMIDDIA RGLRTLEEII GQPVTCSAAA GWRADQKVIE AKEAFHLRYN SDCRGAMPFR PLLESGNPGT AQIPVTLPTW DEVIGRDVKA EDFNGWLLNR ILRDKGTPVY TIHAEVEGCA YQHNFVDLLK RAAQEGVTFC PLSELLSETL PLGQVVRGNI AGREGWLGCQ QIAGSR //