ID   ARNB_SALPA              Reviewed;         379 AA.
AC   Q5PNA4;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   25-MAY-2022, entry version 97.
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=SPA0566;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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=AAV76568.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000026; AAV76568.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q5PNA4; -.
DR   SMR; Q5PNA4; -.
DR   EnsemblBacteria; AAV76568; AAV76568; SPA0566.
DR   KEGG; spt:SPA0566; -.
DR   HOGENOM; CLU_033332_0_3_6; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00032; UER00493.
DR   Proteomes; UP000008185; 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_0000110026"
FT   MOD_RES         182
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01167"
SQ   SEQUENCE   379 AA;  41191 MW;  C894D1D84A266ECA CRC64;
     MLDFLPFSRP AMGAEELAAV KTVLDSGWIT TGPKNQELEA AFCRLTGNQY AVAVSSATAG
     MHIALMALGI GEGDEVITPS MTWVSTLNMI VLLGANPVMV 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