ARNB_ESCF3
ID ARNB_ESCF3 Reviewed; 379 AA.
AC B7LM78;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase {ECO:0000255|HAMAP-Rule:MF_01167};
DE EC=2.6.1.87 {ECO:0000255|HAMAP-Rule:MF_01167};
DE AltName: Full=UDP-(beta-L-threo-pentapyranosyl-4''-ulose diphosphate) aminotransferase {ECO:0000255|HAMAP-Rule:MF_01167};
DE Short=UDP-Ara4O aminotransferase {ECO:0000255|HAMAP-Rule:MF_01167};
DE AltName: Full=UDP-4-amino-4-deoxy-L-arabinose aminotransferase {ECO:0000255|HAMAP-Rule:MF_01167};
GN Name=arnB {ECO:0000255|HAMAP-Rule:MF_01167}; OrderedLocusNames=EFER_0916;
OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
CC -!- FUNCTION: Catalyzes the conversion of UDP-4-keto-arabinose (UDP-Ara4O)
CC to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N). The modified
CC arabinose is attached to lipid A and is required for resistance to
CC polymyxin and cationic antimicrobial peptides. {ECO:0000255|HAMAP-
CC Rule:MF_01167}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + UDP-4-amino-4-deoxy-beta-L-arabinose = L-
CC glutamate + UDP-beta-L-threo-pentopyranos-4-ulose;
CC Xref=Rhea:RHEA:24710, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58708, ChEBI:CHEBI:58710; EC=2.6.1.87;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01167};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01167};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-
CC arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from
CC UDP-alpha-D-glucuronate: step 2/3. {ECO:0000255|HAMAP-Rule:MF_01167}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01167}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01167}.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. ArnB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01167}.
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DR EMBL; CU928158; CAQ88451.1; -; Genomic_DNA.
DR RefSeq; WP_000064515.1; NC_011740.1.
DR AlphaFoldDB; B7LM78; -.
DR SMR; B7LM78; -.
DR EnsemblBacteria; CAQ88451; CAQ88451; EFER_0916.
DR KEGG; efe:EFER_0916; -.
DR HOGENOM; CLU_033332_0_3_6; -.
DR OMA; IVNHGMY; -.
DR OrthoDB; 1722208at2; -.
DR BioCyc; EFER585054:EFER_RS04690-MON; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00032; UER00493.
DR Proteomes; UP000000745; Chromosome.
DR GO; GO:0099620; F:UDP-4-amino-4-deoxy-L-arabinose aminotransferase; IEA:UniProtKB-EC.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR CDD; cd00616; AHBA_syn; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_01167; ArnB_transfer; 1.
DR InterPro; IPR022850; ArnB_NH2Trfase.
DR InterPro; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244; PTHR30244; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Antibiotic resistance; Lipid A biosynthesis;
KW Lipid biosynthesis; Lipid metabolism; Lipopolysaccharide biosynthesis;
KW Pyridoxal phosphate; Transferase.
FT CHAIN 1..379
FT /note="UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate
FT aminotransferase"
FT /id="PRO_1000137958"
FT MOD_RES 182
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01167"
SQ SEQUENCE 379 AA; 41624 MW; 80EEE3A100FD2C51 CRC64;
MSNFLPFSRP AMGAEELAAV KEVLESGWIT TGPKNLALED AFIQLTGNQY AIAVSSATAG
MHITLMALEI GPGDEVITPS MTWVSTLNMI SLLGATPVMV DVDRDTLMVT PEIVEAAITP
RTKAIIPVHY AGAPADTNAL YAIAERHGIA VIEDAAHAVG TYYKGQHVGA RGTAIFSFHA
IKNITCAEGG LVVTDDESLA RQLRTLKFHG LGVDAYDRQT WGRAPQAEVL TPGYKYNLTD
INAAIALTQL HKLEQLNARR HDIATQYQHA LVNLPFQPLA LPAWPHIHSW HLFIIRVDEQ
RCGINRDTLM EALKEKGIGT GLHFRAAHTQ KYYRQHFPDL SLPNTEWNSE RICSLPLFPD
MTNADAERVI TALHQLAGQ
