ID ARND_SHIFL Reviewed; 296 AA. AC Q83KB7; Q7C0R3; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 126. 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=SF2335, S2468; OS Shigella flexneri. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=623; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=301 / Serotype 2a; RX PubMed=12384590; DOI=10.1093/nar/gkf566; RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.; RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity RT through comparison with genomes of Escherichia coli K12 and O157."; RL Nucleic Acids Res. 30:4432-4441(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700930 / 2457T / Serotype 2a; RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003; RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.; RT "Complete genome sequence and comparative genomics of Shigella flexneri RT serotype 2a strain 2457T."; RL Infect. Immun. 71:2775-2786(2003). 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; AE005674; AAN43849.1; -; Genomic_DNA. DR EMBL; AE014073; AAP17668.1; -; Genomic_DNA. DR RefSeq; NP_708142.1; NC_004337.2. DR RefSeq; WP_000169701.1; NZ_WPGW01000032.1. DR AlphaFoldDB; Q83KB7; -. DR SMR; Q83KB7; -. DR STRING; 198214.SF2335; -. DR PaxDb; 198214-SF2335; -. DR GeneID; 1025486; -. DR KEGG; sfl:SF2335; -. DR KEGG; sfx:S2468; -. DR PATRIC; fig|198214.7.peg.2798; -. DR HOGENOM; CLU_084199_0_0_6; -. DR UniPathway; UPA00030; -. DR UniPathway; UPA00036; UER00496. DR Proteomes; UP000001006; Chromosome. DR Proteomes; UP000002673; 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_0000383545" FT DOMAIN 2..260 FT /note="NodB homology" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01870" SQ SEQUENCE 296 AA; 33064 MW; C162658450D49B2E CRC64; MTKVGLRIDV DAFRGTREGV PRLLEILSKH NIQASIFFSV GPDNMGRHLW RLVKPQFLWK MLRSNAASLY GWDILLAGTA WPGKEIGHAN ADIIREAAKH HEVGLHAWDH HAWQARSGNW DRQTMIDDIA RGLRTLEEII GQPVTCSAAA GWRADQKVIE AKEAFHLRYN SDCRGAIPFR PLLESGNPGT AQIPVTLPTW DEVIGRDVKA EDFNGWLLNR ILRDKGTPVY TIHAEVEGCA YQHNFVDLLK RAAQEGVTFC PLSELLSETL PLGQVVRGNI AGREGWLGCQ QIAGSR //