ARNB_YERPS
ID ARNB_YERPS Reviewed; 384 AA.
AC Q7BF87; Q66A02;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 107.
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=YPTB2330;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=32777 / IP2777 / Serotype O1:b;
RX PubMed=15583148; DOI=10.1099/mic.0.27426-0;
RA Marceau M.B., Sebbane F., Ewann F., Collyn F., Lindner B., Campos M.A.,
RA Bengoechea J.-A., Simonet M.;
RT "The pmrF polymyxin-resistance operon of Yersinia pseudotuberculosis is
RT upregulated by the PhoP-PhoQ two-component system but not by PmrA-PmrB, and
RT is not required for virulence.";
RL Microbiology 150:3947-3957(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(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 -!- INDUCTION: Activated by low magnesium concentrations, via the two-
CC component regulatory system PhoP/PhoQ. {ECO:0000269|PubMed:15583148}.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. ArnB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01167}.
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DR EMBL; AF336802; AAK69640.1; -; Genomic_DNA.
DR EMBL; BX936398; CAH21568.1; -; Genomic_DNA.
DR RefSeq; WP_002211825.1; NZ_CP009712.1.
DR AlphaFoldDB; Q7BF87; -.
DR SMR; Q7BF87; -.
DR EnsemblBacteria; CAH21568; CAH21568; YPTB2330.
DR GeneID; 66841236; -.
DR KEGG; ypo:BZ17_124; -.
DR KEGG; yps:YPTB2330; -.
DR PATRIC; fig|273123.14.peg.133; -.
DR OMA; IVNHGMY; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00032; UER00493.
DR Proteomes; UP000001011; 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 2: Evidence at transcript level;
KW Aminotransferase; Antibiotic resistance; Lipid A biosynthesis;
KW Lipid biosynthesis; Lipid metabolism; Lipopolysaccharide biosynthesis;
KW Pyridoxal phosphate; Transferase.
FT CHAIN 1..384
FT /note="UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate
FT aminotransferase"
FT /id="PRO_0000110031"
FT MOD_RES 182
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01167"
SQ SEQUENCE 384 AA; 42246 MW; 054EEDA6DAE9F1C3 CRC64;
MQSFLPFSRP AIGSEEINAV ANVLGSGWIT TGPQNHQLET DFCQIFGCKH AIAVCSATAG
MHITLLALGI GPGDEVITPS QTWVSTINMI VLLGAEPVMV DVDRDTLMVN AAAIEAAITP
NTKAIIPVHY AGAPCDLDAL RQISQRHGIP LIEDAAHAVG TRYRDQWIGE QGTAIFSFHA
IKNITCAEGG LVATDDDELA ARVRRLKFHG LGVDAFDRQI QGRSPQAEVV EPGYKYNLSD
IHAAIAVVQL RRLPEINARR QALVASYHKA LAHLPLQPLA LPHYSHQHAW HLFMVRVDEE
RCGISRDQLM ACLKDMGIGS GLHFRAVHSQ KYYRERYPHL CLPNTEWNSA RLCTLPLFPD
MLDSDIERVA NALTTIIGSH RVTK
