ID ARND_PSEAB Reviewed; 295 AA. AC Q02R26; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2006, sequence version 1. DT 27-MAR-2024, entry version 88. 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=PA14_18340; OS Pseudomonas aeruginosa (strain UCBPP-PA14). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208963; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UCBPP-PA14; RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90; RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S., RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G., RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.; RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is RT combinatorial."; RL Genome Biol. 7:R90.1-R90.14(2006). 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; CP000438; ABJ12789.1; -; Genomic_DNA. DR RefSeq; WP_003138080.1; NZ_CP034244.1. DR AlphaFoldDB; Q02R26; -. DR SMR; Q02R26; -. DR KEGG; pau:PA14_18340; -. DR PseudoCAP; PA14_18340; -. DR HOGENOM; CLU_084199_0_0_6; -. DR BioCyc; PAER208963:G1G74-1513-MONOMER; -. DR UniPathway; UPA00030; -. DR UniPathway; UPA00036; UER00496. DR Proteomes; UP000000653; 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 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. FT CHAIN 1..295 FT /note="Probable 4-deoxy-4-formamido-L-arabinose- FT phosphoundecaprenol deformylase ArnD" FT /id="PRO_0000383522" FT DOMAIN 2..260 FT /note="NodB homology" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01870" SQ SEQUENCE 295 AA; 32906 MW; CFE955C4565A0E27 CRC64; MIQAGLRIDV DTFRGTRDGV PRLLDLLDEA GLKATFFFSV GPDNMGRHLW RLARPAFFWK MLRSRAASLY GWDILLAGTA WPGKPIGREL GPLMRRTQAA GHEVGLHAWD HHAWQTHVGV WSAQQLGEQI RRGSDCLADI LGQPVRCSAA AGWRADGRVV EAKQPFGFRY NSDCRGRGAF RPRLADGSPG IPQVPVNLPT FDEVVGPGLP REAYNDFILE RFAAGRDNVY TIHAEVEGLL LAPAFRELLR RAERRGIRFR PLGELLPDDP RSLPLAELVR GRLAGREGWL GVRQP //