ARNB_SHIBS
ID ARNB_SHIBS Reviewed; 379 AA.
AC Q31YK4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 25-MAY-2022, entry version 94.
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=SBO_2290;
OS Shigella boydii serotype 4 (strain Sb227).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300268;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sb227;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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=ABB66854.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000036; ABB66854.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_001388277.1; NC_007613.1.
DR AlphaFoldDB; Q31YK4; -.
DR SMR; Q31YK4; -.
DR EnsemblBacteria; ABB66854; ABB66854; SBO_2290.
DR KEGG; sbo:SBO_2290; -.
DR HOGENOM; CLU_033332_0_3_6; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00032; UER00493.
DR Proteomes; UP000007067; 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_0000380545"
FT MOD_RES 182
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01167"
SQ SEQUENCE 379 AA; 41642 MW; 0028895E570EB8C6 CRC64;
MSEFLPFSRP AMGVEELAAV KEVLESGWIT TGPKNQALEQ AFCQLTGNQH AIAVSSATAG
MHITLMALEI GKGDEVITPS LTWVSTLNMI SLLGATPVMV DVDRDTLMVT PEAIESAITP
RTKAIIPVHY AGAPADIDAI RAIGERYGIA VIEDAAHAVG TYYKGRHIGA KGTAIFSFHA
IKNITCAEGG LIVTDNENLA RQLRMLKFHG LGVDAYDRQT WGRAPQAEVL TPGYKYNLTD
INAAIALTQL AKLEHLNTRR REIAQQYQQA LAALPFQPLS LPAWPHVHAW HLFIIRVDEQ
RCGISRDALM EALKERGIGT GLHFRAAHTQ KYYRERFPTL SLPNTEWNSE RICSLPLFPD
MTTADADRVI TALQQLAGQ
