ARNB_ECOLI
ID ARNB_ECOLI Reviewed; 385 AA.
AC P77690; Q8KRQ3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase;
DE EC=2.6.1.87 {ECO:0000269|PubMed:12704196};
DE AltName: Full=Polymyxin resistance protein PmrH;
DE AltName: Full=UDP-(beta-L-threo-pentapyranosyl-4''-ulose diphosphate) aminotransferase;
DE Short=UDP-Ara4O aminotransferase;
DE AltName: Full=UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
GN Name=arnB; Synonyms=pmrH, yfbE; OrderedLocusNames=b2253, JW5372;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Breazeale S.D., Ribeiro A.A., McClerren A.L., Raetz C.R.H.;
RT "Enzymatic synthesis of novel UDP-sugars involved in the Escherichia coli
RT modification of lipid A with 4-Amino-4-deoxy-L-arabinose.";
RL FASEB J. 16:A900-A900(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=12704196; DOI=10.1074/jbc.m304043200;
RA Breazeale S.D., Ribeiro A.A., Raetz C.R.H.;
RT "Origin of lipid A species modified with 4-amino-4-deoxy-L-arabinose in
RT polymyxin-resistant mutants of Escherichia coli. An aminotransferase (ArnB)
RT that generates UDP-4-deoxyl-L-arabinose.";
RL J. Biol. Chem. 278:24731-24739(2003).
RN [6]
RP PATHWAY.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=17928292; DOI=10.1074/jbc.m706172200;
RA Yan A., Guan Z., Raetz C.R.H.;
RT "An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin
RT resistance in Escherichia coli.";
RL J. Biol. Chem. 282:36077-36089(2007).
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.
CC {ECO:0000269|PubMed:12704196}.
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:0000269|PubMed:12704196};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
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:0000269|PubMed:17928292}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000269|PubMed:17928292}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8ZNF3}.
CC -!- INDUCTION: Induced by BasR. {ECO:0000250|UniProtKB:Q8ZNF3}.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. ArnB subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC75313.3; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF527386; AAM92146.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75313.3; ALT_INIT; Genomic_DNA.
DR EMBL; AP009048; BAA16076.2; -; Genomic_DNA.
DR PIR; C64996; C64996.
DR RefSeq; NP_416756.5; NC_000913.3.
DR AlphaFoldDB; P77690; -.
DR SMR; P77690; -.
DR BioGRID; 4259180; 238.
DR STRING; 511145.b2253; -.
DR jPOST; P77690; -.
DR PaxDb; P77690; -.
DR PRIDE; P77690; -.
DR EnsemblBacteria; AAC75313; AAC75313; b2253.
DR EnsemblBacteria; BAA16076; BAA16076; BAA16076.
DR GeneID; 947375; -.
DR KEGG; ecj:JW5372; -.
DR KEGG; eco:b2253; -.
DR PATRIC; fig|511145.12.peg.2345; -.
DR EchoBASE; EB3842; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_0_3_6; -.
DR InParanoid; P77690; -.
DR PhylomeDB; P77690; -.
DR BioCyc; EcoCyc:G7166-MON; -.
DR BioCyc; MetaCyc:G7166-MON; -.
DR BRENDA; 2.6.1.87; 2026.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00032; UER00493.
DR PRO; PR:P77690; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; NAS:EcoCyc.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:0099620; F:UDP-4-amino-4-deoxy-L-arabinose aminotransferase; IDA:EcoCyc.
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:0000271; P:polysaccharide biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW Aminotransferase; Antibiotic resistance; Lipid A biosynthesis;
KW Lipid biosynthesis; Lipid metabolism; Lipopolysaccharide biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..385
FT /note="UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate
FT aminotransferase"
FT /id="PRO_0000110018"
FT MOD_RES 188
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q8ZNF3"
SQ SEQUENCE 385 AA; 42238 MW; 2017E3C950FFF4B8 CRC64;
MAEGKAMSEF LPFSRPAMGV EELAAVKEVL ESGWITTGPK NQALEQAFCQ LTGNQHAIAV
SSATAGMHIT LMALKIGKGD EVITPSLTWV STLNMISLLG ATPVMVDVDR DTLMVTPEAI
ESAITPRTKA IIPVHYAGAP ADIDAIRAIG ERYGIAVIED AAHAVGTYYK GRHIGAKGTA
IFSFHAIKNI TCAEGGLIVT DNENLARQLR MLKFHGLGVD AYDRQTWGRA PQAEVLTPGY
KYNLTDINAA IALTQLVKLE HLNTRRREIA QQYQQALAAL PFQPLSLPAW PHVHAWHLFI
IRVDEQRCGI SRDALMEALK ERGIGTGLHF RAAHTQKYYR ERFPTLSLPN TEWNSERICS
LPLFPDMTTA DADHVITALQ QLAGQ
