ARND_ECOLI
ID ARND_ECOLI Reviewed; 296 AA.
AC P76472; Q2MAN3;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 140.
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}; Synonyms=pmrJ, yfbH;
GN OrderedLocusNames=b2256, JW2250;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=15695810; DOI=10.1074/jbc.m414265200;
RA Breazeale S.D., Ribeiro A.A., McClerren A.L., Raetz C.R.H.;
RT "A formyltransferase required for polymyxin resistance in Escherichia coli
RT and the modification of lipid A with 4-amino-4-deoxy-L-arabinose:
RT identification and function of UDP-4-deoxy-4-formamido-L-arabinose.";
RL J. Biol. Chem. 280:14154-14167(2005).
RN [4]
RP PATHWAY.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=17928292; DOI=10.1074/jbc.m706172200;
RA Yan A., Guan Z., Raetz C.R.H.;
RT "An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin
RT resistance in Escherichia coli.";
RL J. Biol. Chem. 282:36077-36089(2007).
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 (Probable). {ECO:0000305|PubMed:15695810}.
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 ECO:0000269|PubMed:15695810};
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-Rule:MF_01870,
CC ECO:0000269|PubMed:17928292}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01870,
CC ECO:0000269|PubMed:17928292}.
CC -!- INDUCTION: Induced by BasR. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family. ArnD
CC deformylase subfamily. {ECO:0000255|HAMAP-Rule:MF_01870}.
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DR EMBL; U00096; AAC75316.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76673.1; -; Genomic_DNA.
DR PIR; F64996; F64996.
DR RefSeq; NP_416759.1; NC_000913.3.
DR RefSeq; WP_000169728.1; NZ_LN832404.1.
DR AlphaFoldDB; P76472; -.
DR BioGRID; 4260498; 208.
DR IntAct; P76472; 1.
DR STRING; 511145.b2256; -.
DR PaxDb; P76472; -.
DR PRIDE; P76472; -.
DR EnsemblBacteria; AAC75316; AAC75316; b2256.
DR EnsemblBacteria; BAE76673; BAE76673; BAE76673.
DR GeneID; 58389479; -.
DR GeneID; 945334; -.
DR KEGG; ecj:JW2250; -.
DR KEGG; eco:b2256; -.
DR PATRIC; fig|1411691.4.peg.4481; -.
DR EchoBASE; EB3845; -.
DR eggNOG; COG0726; Bacteria.
DR HOGENOM; CLU_084199_0_0_6; -.
DR InParanoid; P76472; -.
DR OMA; KFLWKML; -.
DR PhylomeDB; P76472; -.
DR BioCyc; EcoCyc:G7169-MON; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00036; UER00496.
DR PRO; PR:P76472; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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; IMP:EcoCyc.
DR GO; GO:0010041; P:response to iron(III) ion; IEP:EcoCyc.
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 1: Evidence at protein level;
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_0000169176"
FT DOMAIN 2..260
FT /note="NodB homology"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01870"
SQ SEQUENCE 296 AA; 33112 MW; DDD0BEE55581DE3C CRC64;
MTKVGLRIDV DTFRGTREGV PRLLEILSKH NIQASIFFSV GPDNMGRHLW RLVKPQFLWK
MLRSNAASLY GWDILLAGTA WPGKEIGHAN ADIIREAAKH HEVGLHAWDH HAWQARSGNW
DRQTMIDDIA RGLRTLEEII GQPVTCSAAA GWRADQKVIE AKEAFHLRYN SDCRGAMPFR
PLLESGNPGT AQIPVTLPTW DEVIGRDVKA EDFNGWLLNR ILRDKGTPVY TIHAEVEGCA
YQHNFVDLLK RAAQEGVTFC PLSELLSETL PLGQVVRGNI AGREGWLGCQ QIAGSR
