ID   ARNB_SALEP              Reviewed;         379 AA.
AC   B5R270;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 2.
DT   25-MAY-2022, entry version 74.
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=SEN2279;
OS   Salmonella enteritidis PT4 (strain P125109).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P125109;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA   Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA   Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT   gallinarum 287/91 provides insights into evolutionary and host adaptation
RT   pathways.";
RL   Genome Res. 18:1624-1637(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAR33863.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM933172; CAR33863.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001279291.1; NC_011294.1.
DR   AlphaFoldDB; B5R270; -.
DR   SMR; B5R270; -.
DR   KEGG; set:SEN2279; -.
DR   HOGENOM; CLU_033332_0_3_6; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00032; UER00493.
DR   Proteomes; UP000000613; 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_0000380537"
FT   MOD_RES         182
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01167"
SQ   SEQUENCE   379 AA;  41152 MW;  F4FFBC0347681FCF CRC64;
     MSDFLPFSRP AMGAEELAAV KTVLDSGWIT TGPKNQELEA AFCRLTGNQY AVAVSSATAG
     MHIALMALGI GEGDEVITPS MTWVSTLNMI VLLGATPVMV DVDRDTLMVT PEHIEAAITP
     QTKAIIPVHY AGAPADLDAI YALGERYGIP VIEDAAHATG TSYKGRHIGA RGTAIFSFHA
     IKNITCAEGG IVVTDNPQFA DKLRSLKFHG LGVDAWDRQS GGRAPQAEVL APGYKYNLPD
     LNAAIALAQL QKLDALNARR AAIAAQYHQA MADLPFQPLS LPSWEHIHAW HLFIIRVDEA
     RCGITRDALM ASLKTKGIGT GLHFRAAHTQ KYYRERFPTL TLPDTEWNSE RICSLPLFPD
     MTESDFDRVI TALHQIAGQ