ID   ARNB_ENT38              Reviewed;         379 AA.
AC   A4WAM5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 95.
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=Ent638_2079;
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638;
RX   PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA   Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA   Vangronsveld J., Newman L., Monchy S.;
RT   "Genome sequence of the plant growth promoting endophytic bacterium
RT   Enterobacter sp. 638.";
RL   PLoS Genet. 6:E1000943-E1000943(2010).
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; CP000653; ABP60755.1; -; Genomic_DNA.
DR   RefSeq; WP_012017470.1; NC_009436.1.
DR   AlphaFoldDB; A4WAM5; -.
DR   SMR; A4WAM5; -.
DR   STRING; 399742.Ent638_2079; -.
DR   EnsemblBacteria; ABP60755; ABP60755; Ent638_2079.
DR   KEGG; ent:Ent638_2079; -.
DR   eggNOG; COG0399; Bacteria.
DR   HOGENOM; CLU_033332_0_3_6; -.
DR   OMA; IVNHGMY; -.
DR   OrthoDB; 1722208at2; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00032; UER00493.
DR   Proteomes; UP000000230; 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_1000065684"
FT   MOD_RES         182
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01167"
SQ   SEQUENCE   379 AA;  41225 MW;  9F97A5D1CF65A1D7 CRC64;
     MNEFLPFSRP AMGPEELAAV SEVLQSGWIT TGPKNQALEQ AFCALTGNQH SIAVSSATAG
     MHVALMALGI QAGDEVITPS LTWVSTLNMI VLLGAEPVMI DVDHDTLMVT PQAIEAAITP
     RTKAIIPVHY AGAPVDIDAI RAVADRHGIP VIEDAAHAAG TYYKGSHVGN RGTAIFSFHA
     IKNMTCAEGG LIVTDDEQLA NRMRSLKFHG LGVDAFDRQT LGRAPQAEVI SPGYKYNLAD
     INAAIALVQL KKLEKNNARR TEIAERYLTE LANTPFLPLS QPAWAHKHAW HLFIVRVDEA
     TCGISRNGLM DDLKAKGIGT GLHFRAAHTQ KYYRERYPAL VLPNTEWNSD RICSIPLFPT
     MTDDDVTRVI AALRDVAGY