(data stored in ACNUC7421 zone)

HOGENOM: PROMH_1_PE1009

ID   PROMH_1_PE1009                       STANDARD;      PRT;   297 AA.
AC   PROMH_1_PE1009; B4ETL8;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Probable
DE   4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD;
DE   EC=3.5.1 n3; (PROMH_1.PE1009).
GN   Name=arnD; OrderedLocusNames=PMI1046;
OS   PROTEUS MIRABILIS HI4320.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PROMH_1.PE1009.
CC       Proteus mirabilis HI4320 chromosome, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:ARND_PROMH
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
CC       and is required for resistance to polymyxin and cationic
CC       antimicrobial peptides (By similarity).
CC   -!- CATALYTIC ACTIVITY: 4-deoxy-4-formamido-beta-L-arabinose di-
CC       trans,poly-cis-undecaprenyl phosphate + H(2)O = 4-amino-4-deoxy-
CC       alpha-L-arabinose di-trans,poly-cis-undecaprenyl phosphate +
CC       formate.
CC   -!- PATHWAY: Glycolipid biosynthesis; 4-amino-4-deoxy-alpha-L-
CC       arabinose undecaprenyl phosphate biosynthesis; 4-amino-4-deoxy-
CC       alpha-L-arabinose undecaprenyl phosphate from UDP-4-deoxy-4-
CC       formamido-beta-L-arabinose and undecaprenyl phosphate: step 2/2.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis.
CC   -!- SIMILARITY: Belongs to the polysaccharide deacetylase family. ArnD
CC       deformylase subfamily.
CC   -!- GENE_FAMILY: HOG000261199 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B4ETL8; -.
DR   EMBL; AM942759; CAR42272.1; -; Genomic_DNA.
DR   RefSeq; YP_002150796.1; NC_010554.1.
DR   STRING; B4ETL8; -.
DR   GeneID; 6803032; -.
DR   GenomeReviews; AM942759_GR; PMI1046.
DR   OMA; CSAVAGW; -.
DR   ProtClustDB; PRK15394; -.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:EC.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-KW.
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; Polysac_deacetylase.
DR   Gene3D; G3DSA:3.20.20.370; Polysac_deacetylase; 2.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SUPFAM; SSF88713; Glyco_hydro/deAcase_b/a-brl; 1.
DR   HOGENOMDNA; PROMH_1.PE1009; -.
KW   polysaccharide deacetylase;
KW   Antibiotic resistance; Complete proteome; Hydrolase;
KW   Lipid A biosynthesis; Lipid synthesis;
KW   Lipopolysaccharide biosynthesis.
SQ   SEQUENCE   297 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKKVGLRVDV DTYRGTKEGI PQLLDVFNKH NIQASFFFSV GPDNMGRHLW RLLKPKFLWK
     MLRSNAASLY GLDILLAGTA WPGKKIAKNL GYLMKQTQDA GHEVGLHSWD HQGWQAKVGR
     WSTEELMQQV RLGVEALEKA LEKPVKCSAV AGWRADERVL MVKEAFQFDY NSDCRGTHPF
     RPVLENGSIG TVQIPVTLPT YDEVVGTKVK DEDFNQFIID EIKKDQGIPV YTIHTEVEGM
     SKAAQFEQLL AMIANEGIEF CPLSHLLPQD IDMLPMGKVV RSDFPGREGW LGCQQEV
//

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