ARND_PSE14
ID ARND_PSE14 Reviewed; 293 AA.
AC Q48HZ0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=PSPPH_2805;
OS Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=264730;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1448A / Race 6;
RX PubMed=16159782; DOI=10.1128/jb.187.18.6488-6498.2005;
RA Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M.,
RA Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J.,
RA Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., Halpin R.,
RA Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M.,
RA Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A.,
RA Buell R.;
RT "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT 1448A reveals divergence among pathovars in genes involved in virulence and
RT transposition.";
RL J. Bacteriol. 187:6488-6498(2005).
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; CP000058; AAZ37085.1; -; Genomic_DNA.
DR RefSeq; WP_011168796.1; NC_005773.3.
DR AlphaFoldDB; Q48HZ0; -.
DR STRING; 264730.PSPPH_2805; -.
DR EnsemblBacteria; AAZ37085; AAZ37085; PSPPH_2805.
DR KEGG; psp:PSPPH_2805; -.
DR eggNOG; COG0726; Bacteria.
DR HOGENOM; CLU_084199_0_0_6; -.
DR OMA; KFLWKML; -.
DR OrthoDB; 1701876at2; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00036; UER00496.
DR Proteomes; UP000000551; 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..293
FT /note="Probable 4-deoxy-4-formamido-L-arabinose-
FT phosphoundecaprenol deformylase ArnD"
FT /id="PRO_0000383525"
FT DOMAIN 1..259
FT /note="NodB homology"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01870"
SQ SEQUENCE 293 AA; 32728 MW; 9B2E6DF4D161684D CRC64;
MQAGLRIDVD TYRGTREGVP RLLDILDEAQ VKATFFFSVG PDNMGRHLWR LARPTFFWKM
LRSRAASLYG WDILLAGTAW PGKPIGRDLG PLMRRALDAG HEVGLHAWDH HGWQANAGRW
NDRQLTAQIH RGVDCLSDIL GNPVICSAAA GWRADQHVVQ AKQAFGFRYN SDSRGATLFR
PLLADGRLGT PQIPVDLPTF DEVVGPQLQP GAFNEYILNR FAAQRLNVYT IHAEVEGIVM
ADGFRQLLRQ ADAREIEFNP LGQLLPESIE QLPCGQVVRG HLPGREGWLG VQQ