ID   EPMB_BUCAP              Reviewed;         337 AA.
AC   Q44634; O51870;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2002, sequence version 3.
DT   03-AUG-2022, entry version 115.
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; OrderedLocusNames=BUsg_020;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 194-337.
RX   PubMed=9516544; DOI=10.1007/pl00006760;
RA   Clark M.A., Baumann L., Baumann P.;
RT   "Sequence analysis of a 34.7-kb DNA segment from the genome of Buchnera
RT   aphidicola (endosymbiont of aphids) containing groEL, dnaA, the atp operon,
RT   gidA, and rho.";
RL   Curr. Microbiol. 36:158-163(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 194-337.
RA   Anwarul H.K., Moriya S., Baumann P., Yoshikawa H., Ogasawara N.;
RT   "The nucleotide sequence of 60K, tdhF, groES and groEL genes of Buchnera
RT   aphidicola.";
RL   Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the radical SAM superfamily. KamA family.
CC       {ECO:0000305}.
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DR   EMBL; AE013218; AAM67592.1; -; Genomic_DNA.
DR   EMBL; AF008210; AAC38098.1; -; Genomic_DNA.
DR   EMBL; D85628; BAA12848.1; -; Genomic_DNA.
DR   RefSeq; WP_011053558.1; NC_004061.1.
DR   AlphaFoldDB; Q44634; -.
DR   SMR; Q44634; -.
DR   STRING; 198804.BUsg_020; -.
DR   EnsemblBacteria; AAM67592; AAM67592; BUsg_020.
DR   KEGG; bas:BUsg_020; -.
DR   eggNOG; COG1509; Bacteria.
DR   HOGENOM; CLU_032161_2_0_6; -.
DR   OMA; PIWLNTH; -.
DR   OrthoDB; 557227at2; -.
DR   Proteomes; UP000000416; 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   S-adenosyl-L-methionine.
FT   CHAIN           1..337
FT                   /note="L-lysine 2,3-aminomutase"
FT                   /id="PRO_0000172292"
FT   DOMAIN          107..322
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         121
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255"
FT   BINDING         125
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255"
FT   BINDING         128
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         333
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   337 AA;  39502 MW;  D499437C7FDFB536 CRC64;
     MKHYNTKKLN REKDSWLYEI SNSIVEPKKL LKFLHLEKYP KYYDSKPKKV FPFRVPYSFA
     SRMKKNDPKD PLLLQVITKN QEFLNNLQFN EDPVKEKKDI VLPGLLHKYK DRVLWILKTN
     CAINCRYCFR KHFPYEKNKG NKKNWIQILH YISQNIELNE VILSGGDPLM AKDHELLWLI
     TSLSKIKHIK RLRIHTRLPI VIPNRITSDL CQIFSNSVLK IIIVTHINHP QEINEQLSDS
     LLKLKKSNVI LLNQSVLLKN INDNAIILAE LSSRLCENNI IPYYLHILDK VKGTSHFLVS
     NKKAKSIISD LMKMISGFLV PRLVFDNGSK DNKLIII