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ARND_PHOLL
ID   ARND_PHOLL              Reviewed;         297 AA.
AC   Q7N3Q8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=plu2657;
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
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; BX571867; CAE15031.1; -; Genomic_DNA.
DR   RefSeq; WP_011146879.1; NC_005126.1.
DR   AlphaFoldDB; Q7N3Q8; -.
DR   STRING; 243265.plu2657; -.
DR   EnsemblBacteria; CAE15031; CAE15031; plu2657.
DR   GeneID; 24166001; -.
DR   KEGG; plu:plu2657; -.
DR   eggNOG; COG0726; Bacteria.
DR   HOGENOM; CLU_084199_0_0_6; -.
DR   OMA; KFLWKML; -.
DR   OrthoDB; 1701876at2; -.
DR   BioCyc; PLUM243265:PLU_RS13170-MON; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00036; UER00496.
DR   Proteomes; UP000002514; 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; Reference proteome.
FT   CHAIN           1..297
FT                   /note="Probable 4-deoxy-4-formamido-L-arabinose-
FT                   phosphoundecaprenol deformylase ArnD"
FT                   /id="PRO_0000383517"
FT   DOMAIN          2..261
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01870"
SQ   SEQUENCE   297 AA;  33475 MW;  1EAE5892D18DDC1F CRC64;
     MKQIGLRVDV DTYRGTVEGV PKLLKILAKH QIQASFFFSV GPDNMGRHLW RLLRPKFLWK
     MLRSNAASLY GLDILLAGTA WPGKKIAKDL GYLMKQTLNA GHEVGLHAWD HQRWQAKVGR
     WSEAQLTEQV KLGVDALVQA IGQRVTCSAV AGWRADERVL AVKQQFGFDY NSDCRGTHPF
     RPILPDGTLG TVQIPVTLPT YDEVIGIQVK DEDFNQFILD KMKNSQGVPV YTIHTEVEGM
     SKSTEFATLL EMVHQENIQF CALSHLLPEN IQRLPVGRIV RSEFPGREGW LGCQQEA
 
 
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