ARND_SHIB3
ID ARND_SHIB3 Reviewed; 296 AA.
AC B2TW39;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 73.
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=SbBS512_E2632;
OS Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=344609;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 3083-94 / BS512;
RA Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA Jiang L., Ravel J., Sebastian Y.;
RT "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL Submitted (MAY-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}.
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DR EMBL; CP001063; ACD09528.1; -; Genomic_DNA.
DR RefSeq; WP_000169731.1; NC_010658.1.
DR AlphaFoldDB; B2TW39; -.
DR STRING; 344609.SbBS512_E2632; -.
DR PRIDE; B2TW39; -.
DR EnsemblBacteria; ACD09528; ACD09528; SbBS512_E2632.
DR KEGG; sbc:SbBS512_E2632; -.
DR HOGENOM; CLU_084199_0_0_6; -.
DR OMA; KFLWKML; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00036; UER00496.
DR Proteomes; UP000001030; 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 HAMAP; MF_01870; ArnD; 1.
DR InterPro; IPR023557; ArnD.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; SSF88713; 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_0000383542"
FT DOMAIN 2..260
FT /note="NodB homology"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01870"
SQ SEQUENCE 296 AA; 33142 MW; 2981FBF11081C526 CRC64;
MTKVGLRIDV DTFRGTREGV PRLLEILSKH NIQASIFFSV GPDNMGRHLW RLVKPQFLWK
MLRSNAASLY GWDILLAGTA WPGKEIGHAN ADIIREAAKH HEVGLHAWDH HAWQARSGNW
DRQTMIDDIA RGLRTLEEII GQPVTCSAAA GWRADQKVIE AKEAFHLRYN SDCRGAMPFR
PLLESGNPGT AQIPVTLPTW DEVIGRDVKT EDFNGWLLNR ILRDKGTPVY TIHAEVEGCA
YQHNFVDLLK RAAQEGVTFC PLSELLSETL PLGQVVRGNI AGREGWLGCQ QIAGSR
