ARNB_SALTY
ID ARNB_SALTY Reviewed; 385 AA.
AC Q8ZNF3; O52323;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase;
DE EC=2.6.1.87 {ECO:0000269|PubMed:12429098};
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=pbgP, pbgP1, pmrH; OrderedLocusNames=STM2297;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 14028s / SGSG 2262;
RX PubMed=9570402; DOI=10.1046/j.1365-2958.1998.00757.x;
RA Gunn J.S., Lim K.B., Krueger J., Kim K., Guo L., Hackett M., Miller S.I.;
RT "PmrA-PmrB-regulated genes necessary for 4-aminoarabinose lipid A
RT modification and polymyxin resistance.";
RL Mol. Microbiol. 27:1171-1182(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP INDUCTION.
RC STRAIN=ATCC 14028s / SGSG 2262;
RX PubMed=10480935; DOI=10.1074/jbc.274.38.27185;
RA Woesten M.M.S.M., Groisman E.A.;
RT "Molecular characterization of the PmrA regulon.";
RL J. Biol. Chem. 274:27185-27190(1999).
RN [4] {ECO:0007744|PDB:1MDO, ECO:0007744|PDB:1MDX, ECO:0007744|PDB:1MDZ}
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE
RP AND INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, ACTIVE
RP SITE, AND SUBUNIT.
RX PubMed=12429098; DOI=10.1016/s0969-2126(02)00879-1;
RA Noland B.W., Newman J.M., Hendle J., Badger J., Christopher J.A.,
RA Tresser J., Buchanan M.D., Wright T.A., Rutter M.E., Sanderson W.E.,
RA Mueller-Dieckmann H.-J., Gajiwala K.S., Buchanan S.G.;
RT "Structural studies of Salmonella typhimurium ArnB (PmrH) aminotransferase:
RT a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme.";
RL Structure 10:1569-1580(2002).
RN [5] {ECO:0007744|PDB:4OCA}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT ALA-188 IN COMPLEX WITH
RP PYRIDOXAL PHOSPHATE AND SUBSTRATE, FUNCTION, ACTIVE SITE, REACTION
RP MECHANISM, SUBUNIT, AND MUTAGENESIS OF LYS-188.
RX PubMed=24460375; DOI=10.1021/bi4015677;
RA Lee M., Sousa M.C.;
RT "Structural basis for substrate specificity in ArnB. A key enzyme in the
RT polymyxin resistance pathway of Gram-negative bacteria.";
RL Biochemistry 53:796-805(2014).
CC -!- FUNCTION: Catalyzes the conversion of UDP-4-keto-arabinose (UDP-Ara4O)
CC to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) (PubMed:12429098,
CC PubMed:24460375). The modified arabinose is attached to lipid A and is
CC required for resistance to polymyxin and cationic antimicrobial
CC peptides (By similarity). {ECO:0000250, ECO:0000269|PubMed:12429098,
CC ECO:0000269|PubMed:24460375}.
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:12429098};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:12429098};
CC -!- ACTIVITY REGULATION: Inhibited by L-cycloserine.
CC {ECO:0000269|PubMed:12429098}.
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.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12429098,
CC ECO:0000269|PubMed:24460375}.
CC -!- INDUCTION: Induced by BasR. {ECO:0000269|PubMed:10480935}.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. ArnB subfamily.
CC {ECO:0000305}.
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DR EMBL; AF036677; AAC04770.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21198.1; -; Genomic_DNA.
DR RefSeq; NP_461239.3; NC_003197.2.
DR RefSeq; WP_001520579.1; NC_003197.2.
DR PDB; 1MDO; X-ray; 1.70 A; A=1-385.
DR PDB; 1MDX; X-ray; 1.96 A; A=1-385.
DR PDB; 1MDZ; X-ray; 2.07 A; A=1-385.
DR PDB; 4OCA; X-ray; 2.30 A; A=1-385.
DR PDBsum; 1MDO; -.
DR PDBsum; 1MDX; -.
DR PDBsum; 1MDZ; -.
DR PDBsum; 4OCA; -.
DR AlphaFoldDB; Q8ZNF3; -.
DR SMR; Q8ZNF3; -.
DR STRING; 99287.STM2297; -.
DR DrugBank; DB02038; D-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-N,O-cycloserylamide.
DR DrugBank; DB02142; Pyridoxamine-5'-Phosphate.
DR PaxDb; Q8ZNF3; -.
DR EnsemblBacteria; AAL21198; AAL21198; STM2297.
DR GeneID; 1253819; -.
DR KEGG; stm:STM2297; -.
DR HOGENOM; CLU_033332_0_3_6; -.
DR PhylomeDB; Q8ZNF3; -.
DR BioCyc; SENT99287:STM2297-MON; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00032; UER00493.
DR EvolutionaryTrace; Q8ZNF3; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
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: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 3D-structure; Aminotransferase; Antibiotic resistance;
KW Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW Lipopolysaccharide biosynthesis; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..385
FT /note="UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate
FT aminotransferase"
FT /id="PRO_0000110028"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:12429098,
FT ECO:0000305|PubMed:24460375"
FT MOD_RES 188
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:12429098,
FT ECO:0007744|PDB:1MDX, ECO:0007744|PDB:1MDZ"
FT MUTAGEN 188
FT /note="K->A: Loss of covalent pyridoxal phosphate binding."
FT /evidence="ECO:0000269|PubMed:24460375"
FT CONFLICT 285
FT /note="L -> V (in Ref. 2; AAC04770)"
FT /evidence="ECO:0000305"
FT HELIX 20..32
FT /evidence="ECO:0007829|PDB:1MDO"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:1MDO"
FT HELIX 39..52
FT /evidence="ECO:0007829|PDB:1MDO"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:1MDO"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:1MDO"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:1MDO"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:1MDO"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:1MDO"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:1MDO"
FT HELIX 117..123
FT /evidence="ECO:0007829|PDB:1MDO"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:1MDO"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:1MDO"
FT HELIX 143..153
FT /evidence="ECO:0007829|PDB:1MDO"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:1MDX"
FT STRAND 176..183
FT /evidence="ECO:0007829|PDB:1MDO"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:1MDO"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:1MDO"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:1MDO"
FT HELIX 203..212
FT /evidence="ECO:0007829|PDB:1MDO"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:1MDO"
FT HELIX 246..257
FT /evidence="ECO:0007829|PDB:1MDO"
FT HELIX 259..278
FT /evidence="ECO:0007829|PDB:1MDO"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:1MDO"
FT HELIX 305..308
FT /evidence="ECO:0007829|PDB:1MDO"
FT HELIX 312..321
FT /evidence="ECO:0007829|PDB:1MDO"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:1MDO"
FT HELIX 337..342
FT /evidence="ECO:0007829|PDB:1MDO"
FT HELIX 349..355
FT /evidence="ECO:0007829|PDB:1MDO"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:1MDO"
FT HELIX 369..383
FT /evidence="ECO:0007829|PDB:1MDO"
SQ SEQUENCE 385 AA; 41813 MW; DAA6C24FC591FA05 CRC64;
MAEGKMMSDF LPFSRPAMGA EELAAVKTVL DSGWITTGPK NQELEAAFCR LTGNQYAVAV
SSATAGMHIA LMALGIGEGD EVITPSMTWV STLNMIVLLG ANPVMVDVDR DTLMVTPEHI
EAAITPQTKA IIPVHYAGAP ADLDAIYALG ERYGIPVIED AAHATGTSYK GRHIGARGTA
IFSFHAIKNI TCAEGGIVVT DNPQFADKLR SLKFHGLGVD AWDRQSGGRA PQAEVLAPGY
KYNLPDLNAA IALAQLQKLD ALNARRAAIA AQYHQAMADL PFQPLSLPSW EHIHAWHLFI
IRVDEARCGI TRDALMASLK TKGIGTGLHF RAAHTQKYYR ERFPTLTLPD TEWNSERICS
LPLFPDMTES DFDRVITALH QIAGQ
