EPMB_SALTY
ID EPMB_SALTY Reviewed; 342 AA.
AC Q8ZKB8;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=L-lysine 2,3-aminomutase;
DE Short=LAM;
DE EC=5.4.3.-;
DE AltName: Full=EF-P post-translational modification enzyme B;
GN Name=epmB; Synonyms=yjeK; OrderedLocusNames=STM4333;
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 [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 [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=14028s / SGSC 2262, and LT2 / SGSC1412 / ATCC 700720;
RX PubMed=20670890; DOI=10.1016/j.molcel.2010.06.021;
RA Navarre W.W., Zou S.B., Roy H., Xie J.L., Savchenko A., Singer A.,
RA Edvokimova E., Prost L.R., Kumar R., Ibba M., Fang F.C.;
RT "PoxA, YjeK, and elongation factor P coordinately modulate virulence and
RT drug resistance in Salmonella enterica.";
RL Mol. Cell 39:209-221(2010).
CC -!- FUNCTION: With EpmA is involved in the beta-lysylation step of the
CC post-translational modification of translation elongation factor P (EF-
CC P) on 'Lys-34'. EpmB appears to act before EpmA. Displays lysine 2,3-
CC aminomutase activity, producing (R)-beta-lysine from (S)-alpha-lysine
CC (L-lysine) (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysine = D-beta-lysine; Xref=Rhea:RHEA:44148,
CC ChEBI:CHEBI:32551, ChEBI:CHEBI:84138;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are highly attenuated for
CC virulence in mouse models of infection. Salmonella epmA and epmB
CC mutants share extensive phenotypic pleiotropy, including an increased
CC ability to respire under nutrient-limiting conditions,
CC hypersusceptibility to a variety of diverse growth inhibitors, and
CC altered expression of multiple proteins, including several encoded on
CC the SPI-1 pathogenicity island. {ECO:0000269|PubMed:20670890}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. KamA family.
CC {ECO:0000305}.
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DR EMBL; AE006468; AAL23156.1; -; Genomic_DNA.
DR RefSeq; NP_463197.1; NC_003197.2.
DR RefSeq; WP_000940484.1; NC_003197.2.
DR AlphaFoldDB; Q8ZKB8; -.
DR SMR; Q8ZKB8; -.
DR STRING; 99287.STM4333; -.
DR PaxDb; Q8ZKB8; -.
DR EnsemblBacteria; AAL23156; AAL23156; STM4333.
DR GeneID; 1255859; -.
DR KEGG; stm:STM4333; -.
DR PATRIC; fig|99287.12.peg.4559; -.
DR HOGENOM; CLU_032161_2_0_6; -.
DR OMA; PIWLNTH; -.
DR PhylomeDB; Q8ZKB8; -.
DR BioCyc; SENT99287:STM4333-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR022462; EpmB.
DR InterPro; IPR003739; Lys_aminomutase/Glu_NH3_mut.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR30538; PTHR30538; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF004911; DUF160; 1.
DR SFLD; SFLDF00314; L-lysine_2_3-aminomutase_(yjeK; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR TIGRFAMs; TIGR03821; EFP_modif_epmB; 1.
DR TIGRFAMs; TIGR00238; TIGR00238; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Isomerase; Metal-binding; Pyridoxal phosphate;
KW Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..342
FT /note="L-lysine 2,3-aminomutase"
FT /id="PRO_0000419667"
FT DOMAIN 106..329
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 120
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255"
FT BINDING 124
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255"
FT BINDING 127
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255"
FT MOD_RES 332
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 342 AA; 38777 MW; 02D849D144D04389 CRC64;
MAHIVTLNTP LREDWLAQLA DVVTNPDELL HLLQIEADEN LRAGQDARRL FALRVPRAFI
ARMEKGNPDD PLLRQVLTSR DEFIVAPGFS TDPLEEQHSV VPGLLHKYQN RALLLVKGGC
AVNCRYCFRR HFPYAENQGN KRNWTVALEY IAAHPELDEI IFSGGDPLMA KDHELDWLLT
QLEAIKHVKR LRIHSRLPIV IPARITDELV ARFDQSRLQI LLVNHINHAN EVDEAFGLAM
KKLRHVGVTL LNQSVLLRGV NDNARTLANL SNALFDAGVM PYYLHVLDKV QGAAHFMVTD
DEARQIMREL LTLVSGYMVP RLAREIGGEP SKTPLDLQLR QC
