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 24-JAN-2024, entry version 101.
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; Pseudomonadota; 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 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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; TRANSAMINASE; 1.
DR PANTHER; PTHR30244:SF41; UDP-4-AMINO-4-DEOXY-L-ARABINOSE--OXOGLUTARATE AMINOTRANSFERASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 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
//
