ID J3Z4A1_9ENTR Unreviewed; 298 AA.
AC J3Z4A1;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD {ECO:0000256|HAMAP-Rule:MF_01870};
DE EC=3.5.1.n3 {ECO:0000256|HAMAP-Rule:MF_01870};
GN Name=arnD {ECO:0000256|HAMAP-Rule:MF_01870};
GN ORFNames=A359_07490 {ECO:0000313|EMBL:AFP85119.1};
OS secondary endosymbiont of Ctenarytaina eucalypti.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; aphid secondary symbionts.
OX NCBI_TaxID=1199245 {ECO:0000313|EMBL:AFP85119.1, ECO:0000313|Proteomes:UP000003936};
RN [1] {ECO:0000313|EMBL:AFP85119.1, ECO:0000313|Proteomes:UP000003936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ceuc_S {ECO:0000313|EMBL:AFP85119.1};
RX PubMed=22821013; DOI=10.1093/molbev/mss180;
RA Sloan D.B., Moran N.A.;
RT "Genome reduction and co-evolution between the primary and secondary
RT bacterial symbionts of psyllids.";
RL Mol. Biol. Evol. 29:3781-3792(2012).
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:0000256|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:0000256|HAMAP-Rule:MF_01870};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01870}.
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family. ArnD
CC deformylase subfamily. {ECO:0000256|HAMAP-Rule:MF_01870}.
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DR EMBL; CP003546; AFP85119.1; -; Genomic_DNA.
DR AlphaFoldDB; J3Z4A1; -.
DR STRING; 1199245.A359_07490; -.
DR KEGG; sect:A359_07490; -.
DR PATRIC; fig|1199245.3.peg.870; -.
DR HOGENOM; CLU_084199_0_0_6; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00036; UER00496.
DR Proteomes; UP000003936; 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:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
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 GO; GO:0045493; P:xylan catabolic process; 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 {ECO:0000256|ARBA:ARBA00023251, ECO:0000256|HAMAP-
KW Rule:MF_01870}; Carbohydrate metabolism {ECO:0000313|EMBL:AFP85119.1};
KW Glycosidase {ECO:0000313|EMBL:AFP85119.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01870, ECO:0000313|EMBL:AFP85119.1};
KW Lipid A biosynthesis {ECO:0000256|ARBA:ARBA00022556, ECO:0000256|HAMAP-
KW Rule:MF_01870};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_01870};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_01870};
KW Lipopolysaccharide biosynthesis {ECO:0000256|ARBA:ARBA00022985,
KW ECO:0000256|HAMAP-Rule:MF_01870};
KW Polysaccharide degradation {ECO:0000313|EMBL:AFP85119.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003936};
KW Xylan degradation {ECO:0000313|EMBL:AFP85119.1}.
FT DOMAIN 3..261
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 298 AA; 33204 MW; 7C9DEBAB49D63130 CRC64;
MLKNVGLRID VDTWRGTRAG VPCLLDILAA QKIKSTFFFS VGPDNMGRHF WRLTKPQFLM
KMLRSRVVSL YSWKILLAGT AWPGRKIGQG LAAQIRAAAA DHEVGMHAWD HFAWQTWAGT
WDNAELTKQI RLAKDALTNI IEQPVTCSAA AGWRADNRVL QAKQPFGFFY NSDCRGTSLF
RPLLPNGDWG TVQIPVTQPT FDEIIGHTVS LAGYNRFILD SIKADHGTPV YTIHAEVEGI
ALSGMFQELL WMARAEGIRF CPLGELIPQD ATVLPVGHIV RGVIPGREGW VGCQRLLK
//
