ID   ARND_YERPS              Reviewed;         301 AA.
AC   Q7BF86; Q66A05;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 103.
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=YPTB2327;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=32777 / IP2777 / Serotype O1:b;
RX   PubMed=15583148; DOI=10.1099/mic.0.27426-0;
RA   Marceau M.B., Sebbane F., Ewann F., Collyn F., Lindner B., Campos M.A.,
RA   Bengoechea J.-A., Simonet M.;
RT   "The pmrF polymyxin-resistance operon of Yersinia pseudotuberculosis is
RT   upregulated by the PhoP-PhoQ two-component system but not by PmrA-PmrB, and
RT   is not required for virulence.";
RL   Microbiology 150:3947-3957(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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   -!- INDUCTION: Activated by low magnesium concentrations, via the two-
CC       component regulatory system PhoP/PhoQ. {ECO:0000269|PubMed:15583148}.
CC   -!- SIMILARITY: Belongs to the polysaccharide deacetylase family. ArnD
CC       deformylase subfamily. {ECO:0000255|HAMAP-Rule:MF_01870}.
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DR   EMBL; AF336802; AAK69643.1; -; Genomic_DNA.
DR   EMBL; BX936398; CAH21565.1; -; Genomic_DNA.
DR   RefSeq; WP_002211822.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q7BF86; -.
DR   SMR; Q7BF86; -.
DR   GeneID; 66841239; -.
DR   KEGG; ypo:BZ17_127; -.
DR   KEGG; yps:YPTB2327; -.
DR   PATRIC; fig|273123.14.peg.136; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00036; UER00496.
DR   Proteomes; UP000001011; 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   2: Evidence at transcript level;
KW   Antibiotic resistance; Hydrolase; Lipid A biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Lipopolysaccharide biosynthesis.
FT   CHAIN           1..301
FT                   /note="Probable 4-deoxy-4-formamido-L-arabinose-
FT                   phosphoundecaprenol deformylase ArnD"
FT                   /id="PRO_0000383556"
FT   DOMAIN          2..261
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01870"
SQ   SEQUENCE   301 AA;  33504 MW;  ABA3A1132D09A864 CRC64;
     MKQVGLRIDV DTYRGTQYGV PSLLTVLEKH DIRASFFFSV GPDNMGRHLW RLFRPRFLWK
     MLRSNAASLY GWDILLAGTA WPGKKIAKDF GPLMKAAAMA GHEVGLHAWD HQGWQANVAS
     WSQQQLTEQV QRGVDTLQQS IGQPISCSAA AGWRADERVL AVKQQFDFSY NSDCRGTHPF
     RPLLPNGSLG SVQIPVTLPT YDEVVGGEVQ AENFNDFIID AILRDSGVSV YTIHAEVEGM
     SQAAMFEQLL MRAKQQDIEF CPLSKLLPSD LQLLPVGKVI RAAFPGREGW LGCQSDIKDA
     E
//