ID   ARNB_ECOUT              Reviewed;         379 AA.
AC   Q1R9G2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 2.
DT   25-MAY-2022, entry version 91.
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=UTI89_C2535;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABE08002.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000243; ABE08002.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011076488.1; NC_007946.1.
DR   AlphaFoldDB; Q1R9G2; -.
DR   SMR; Q1R9G2; -.
DR   EnsemblBacteria; ABE08002; ABE08002; UTI89_C2535.
DR   KEGG; eci:UTI89_C2535; -.
DR   HOGENOM; CLU_033332_0_3_6; -.
DR   OMA; IVNHGMY; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00032; UER00493.
DR   Proteomes; UP000001952; 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_0000380534"
FT   MOD_RES         182
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01167"
SQ   SEQUENCE   379 AA;  41591 MW;  02BD39B9E854B078 CRC64;
     MSGFLPFSRP AMGVEELAAV KEVLESGWIT TGPKNQALEQ AFCQLTGNQH AIAVSSATAG
     MHITLMALEI GKGDEVITPS LTWVSTLNMI SLLGATPVMV DVDRDTLMVT PEAIEAAITP
     RTKAIIPVHY AGAPADIDAI RAIGERYGIA VIEDAAHAVG TYYKGRHIGA KGTAIFSFHA
     IKNITCAEGG LIVTDNENLA RQLRMLKFHG LGVDAYDRHT WGRAPQAEVL TPGYKYNLTD
     INAAIALTQL VKLEHLNTRR REIAQQYQQA LAALPFQPLS LPAWPHVHAW HLFIIRVDEQ
     RCGISRDALM EALKERGIGT GLHFRAAHTQ KYYRERFPTL SLPNTEWNSE RICSLPLFPD
     MTTADADRVI TALQQLAGQ