ID ARND_ECOLC Reviewed; 296 AA. AC B1IXT1; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, 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=EcolC_1393; OS Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / OS WDCM 00012 / Crooks). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=481805; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / RC Crooks; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C., RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Ingram L., Richardson P.; RT "Complete sequence of Escherichia coli C str. ATCC 8739."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. 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; CP000946; ACA77057.1; -; Genomic_DNA. DR RefSeq; WP_000169728.1; NZ_MTFT01000028.1. DR AlphaFoldDB; B1IXT1; -. DR SMR; B1IXT1; -. DR GeneID; 75205694; -. DR KEGG; ecl:EcolC_1393; -. DR HOGENOM; CLU_084199_0_0_6; -. DR UniPathway; UPA00030; -. DR UniPathway; UPA00036; UER00496. 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. FT CHAIN 1..296 FT /note="Probable 4-deoxy-4-formamido-L-arabinose- FT phosphoundecaprenol deformylase ArnD" FT /id="PRO_0000383496" FT DOMAIN 2..260 FT /note="NodB homology" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01870" SQ SEQUENCE 296 AA; 33112 MW; DDD0BEE55581DE3C CRC64; MTKVGLRIDV DTFRGTREGV PRLLEILSKH NIQASIFFSV GPDNMGRHLW RLVKPQFLWK MLRSNAASLY GWDILLAGTA WPGKEIGHAN ADIIREAAKH HEVGLHAWDH HAWQARSGNW DRQTMIDDIA RGLRTLEEII GQPVTCSAAA GWRADQKVIE AKEAFHLRYN SDCRGAMPFR PLLESGNPGT AQIPVTLPTW DEVIGRDVKA EDFNGWLLNR ILRDKGTPVY TIHAEVEGCA YQHNFVDLLK RAAQEGVTFC PLSELLSETL PLGQVVRGNI AGREGWLGCQ QIAGSR //