ID   ARND_SERP5              Reviewed;         301 AA.
AC   A8GDR8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=Spro_2157;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000826; ABV41258.1; -; Genomic_DNA.
DR   RefSeq; WP_012144889.1; NC_009832.1.
DR   AlphaFoldDB; A8GDR8; -.
DR   SMR; A8GDR8; -.
DR   STRING; 399741.Spro_2157; -.
DR   EnsemblBacteria; ABV41258; ABV41258; Spro_2157.
DR   KEGG; spe:Spro_2157; -.
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   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..301
FT                   /note="Probable 4-deoxy-4-formamido-L-arabinose-
FT                   phosphoundecaprenol deformylase ArnD"
FT                   /id="PRO_0000383540"
FT   DOMAIN          2..261
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01870"
SQ   SEQUENCE   301 AA;  33692 MW;  8018A168DB513983 CRC64;
     MKKVGLRVDV DTFSGTREGV PQLLELFDKY NIQASFFFSV GPDNMGRHLW RLLRPKFLWK
     MLRSNAASLY GWDILLAGTA WPGRNIARAL GPLMKLTAQA GHEVGLHAWD HQGWQAKVGR
     WSEAQLMQQV QLGVDALANS TGQPVKCSAV AGWRADTRVL EVKQRFGFHY NSDCRGTHPF
     RPVLSDGRLG TVQIPVTLPT FDEVIGSEVS MNDFNDYILR EIENDRGVPV YTIHTEVEGM
     SQAAMFEQLL LRAQRQGIEF CPLSALLPQD LASLPLGRVE RAPFPGREGW LGCQTDVKDD
     S