ID   ARND_ECOSE              Reviewed;         296 AA.
AC   B6I7J9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 76.
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=ECSE_2515;
OS   Escherichia coli (strain SE11).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=409438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SE11;
RX   PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA   Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T.,
RA   Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT   "Complete genome sequence and comparative analysis of the wild-type
RT   commensal Escherichia coli strain SE11 isolated from a healthy adult.";
RL   DNA Res. 15:375-386(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}.
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DR   EMBL; AP009240; BAG78039.1; -; Genomic_DNA.
DR   RefSeq; WP_000169737.1; NC_011415.1.
DR   AlphaFoldDB; B6I7J9; -.
DR   SMR; B6I7J9; -.
DR   GeneID; 75172387; -.
DR   KEGG; ecy:ECSE_2515; -.
DR   HOGENOM; CLU_084199_0_0_6; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00036; UER00496.
DR   Proteomes; UP000008199; 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.
FT   CHAIN           1..296
FT                   /note="Probable 4-deoxy-4-formamido-L-arabinose-
FT                   phosphoundecaprenol deformylase ArnD"
FT                   /id="PRO_0000383498"
FT   DOMAIN          2..260
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01870"
SQ   SEQUENCE   296 AA;  33112 MW;  DDC064897DFD2C3C CRC64;
     MTKVGLRIDV DTFRGTREGV PRLLEILSKH NIQASIFFSV GPDNMGRHLW RLVKPQFLWK
     MLRSNAASLY GWDILLAGTA WPGKEIGHAN ADIIREAAKH HEVGLHAWDH HAWQARSGNW
     DRQTMIDDIA RGLRTLEEII GQPVTCSAAA GWRADQQVIE AKEAFHLRYN SDCRGAMPFR
     PLLESGNPGT AQIPVTLPTW DEVIGRDVKA EDFNGWLLNR ILRDKGTPVY TIHAEVEGCA
     YQHNFVDLLK RAAQEGVTFC PLSELLSETL PLGQVVRGNI AGREGWLGCQ QIAGSR
//