ID   ARNB_ECOHS              Reviewed;         379 AA.
AC   A8A2C0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
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=EcHS_A2398;
OS   Escherichia coli O9:H4 (strain HS).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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; CP000802; ABV06674.1; -; Genomic_DNA.
DR   RefSeq; WP_001295286.1; NC_009800.1.
DR   AlphaFoldDB; A8A2C0; -.
DR   SMR; A8A2C0; -.
DR   KEGG; ecx:EcHS_A2398; -.
DR   HOGENOM; CLU_033332_0_3_6; -.
DR   OMA; IVNHGMY; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00032; UER00493.
DR   Proteomes; UP000001123; 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_1000065683"
FT   MOD_RES         182
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01167"
SQ   SEQUENCE   379 AA;  41650 MW;  3BB025C28508837E CRC64;
     MSEFLPFSRP AMGVEELAAV KEVLESGWIT TGPKNQALEQ AFCQLTGNQH AIAVSSATAG
     MHITLMALKI GKGDEVITPS LTWVSTLNMI SLLGATPVMV DVDRDTLMVT PEAIESAITP
     RTKAIIPVHY AGAPADIDAI RAIGERYGIA VIEDAAHAVG TYYKGRHIGA KGTAIFSFHA
     IKNITCAEGG LIVTDNENLA RQLRMLKFHG LGVDAYDRQT WGRAPQAEVL TPGYKYNLTD
     INAAIALTQL VKLEHLNTRR REIAQQYQQA LAALPFQPLS LPAWPHVHAW HLFIIRVDEQ
     RCGISRDALM EALKERGIGT GLHFRAAHTQ KYYRERFPTL SLPNTEWNSE RICSLPLFPD
     MTTADADHVI TALQQLAGQ