ID ARND_SALPK Reviewed; 299 AA.
AC B5BCP5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
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}; OrderedLocusNames=SSPA0527;
OS Salmonella paratyphi A (strain AKU_12601).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=554290;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AKU_12601;
RX PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA Mungall K., Dougan G., Parkhill J.;
RT "Pseudogene accumulation in the evolutionary histories of Salmonella
RT enterica serovars Paratyphi A and Typhi.";
RL BMC Genomics 10:36-36(2009).
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; FM200053; CAR58656.1; -; Genomic_DNA.
DR RefSeq; WP_000169759.1; NC_011147.1.
DR AlphaFoldDB; B5BCP5; -.
DR SMR; B5BCP5; -.
DR KEGG; sek:SSPA0527; -.
DR HOGENOM; CLU_084199_0_0_6; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00036; UER00496.
DR Proteomes; UP000001869; 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..299
FT /note="Probable 4-deoxy-4-formamido-L-arabinose-
FT phosphoundecaprenol deformylase ArnD"
FT /id="PRO_0000383535"
FT DOMAIN 2..260
FT /note="NodB homology"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01870"
SQ SEQUENCE 299 AA; 33048 MW; 48A039CEC4974A9E CRC64;
MTKVGLRIDV DTLRGTREGV PRLLATLHRH GVQASFFFSV GPDNMGRHLW RLIKPRFLWK
MLRSNAASLY GWDILLAGTA WPGKNIGNAN AGIIRETATY HETGLHAWDH HAWQTHSGHW
SIRQLEEDIA RGITALEAII GKPVTCSAAA GWRADGRVVR AKEPFNLRYN SDCRGTTLFR
PLLMPGQTGT PQIPVTLPTW DEVIGPAVQA QSFNTWIISR MLQDKGTPVY TIHAEVEGIV
HQPLFEDLLV RARDAGITFC PLGELLPASP ESLPLGQIVR GHIPGREGWL GCQQAVSAS
//
