ID   EPMB_BUCBP              Reviewed;         340 AA.
AC   Q89B32;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=bbp_022;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO26765.1; -; Genomic_DNA.
DR   RefSeq; WP_011091166.1; NC_004545.1.
DR   AlphaFoldDB; Q89B32; -.
DR   SMR; Q89B32; -.
DR   STRING; 224915.bbp_022; -.
DR   EnsemblBacteria; AAO26765; AAO26765; bbp_022.
DR   GeneID; 56470566; -.
DR   KEGG; bab:bbp_022; -.
DR   eggNOG; COG1509; Bacteria.
DR   HOGENOM; CLU_032161_2_0_6; -.
DR   OMA; PIWLNTH; -.
DR   OrthoDB; 557227at2; -.
DR   Proteomes; UP000000601; 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   PIRSF; PIRSF004911; DUF160; 1.
DR   SFLD; SFLDF00314; L-lysine_2_3-aminomutase_(yjeK; 1.
DR   SFLD; SFLDG01070; PLP-dependent; 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..340
FT                   /note="L-lysine 2,3-aminomutase"
FT                   /id="PRO_0000172293"
FT   DOMAIN          106..321
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   340 AA;  39661 MW;  28499EFBE8CF8244 CRC64;
     MLNKKIKKNH KEDWITELTN AITNPDELLR TLNLKSNTKY FKNIQVQKLF SLRVPKTFVS
     RMKKNDPFDP LLLQILPHTK ELKNNHNFVQ DPLEETKNVI IPGLIRKYNN RILLLLKTNC
     AINCRYCFRR YFPYSQHPGN KENLNLAIQY IKNQTDLNEV ILSGGDPLMA KDHEIQWIVN
     TLSNIYHIKR LRIHTRLPIV IPSRITNNLC KILSTTRLKI LIVTHINHAQ EINHELQYNI
     NKLHKLGITL LNQSVLLRGI NDNAKILSQL SNKLFDINIL PYYLHILDKV KSTTHFYVSE
     KQASIIVVEL LSMISGFLVP KLVCEHPGKN SKIYINLNMK