ID   EPMB_HAEIN              Reviewed;         338 AA.
AC   P44641;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=HI_0329;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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; L42023; AAC21990.1; -; Genomic_DNA.
DR   PIR; B64148; B64148.
DR   RefSeq; NP_438493.1; NC_000907.1.
DR   RefSeq; WP_005691796.1; NC_000907.1.
DR   AlphaFoldDB; P44641; -.
DR   SMR; P44641; -.
DR   STRING; 71421.HI_0329; -.
DR   EnsemblBacteria; AAC21990; AAC21990; HI_0329.
DR   KEGG; hin:HI_0329; -.
DR   PATRIC; fig|71421.8.peg.346; -.
DR   eggNOG; COG1509; Bacteria.
DR   HOGENOM; CLU_032161_2_0_6; -.
DR   OMA; VTNQCAM; -.
DR   PhylomeDB; P44641; -.
DR   BioCyc; HINF71421:G1GJ1-345-MON; -.
DR   Proteomes; UP000000579; 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; 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..338
FT                   /note="L-lysine 2,3-aminomutase"
FT                   /id="PRO_0000172289"
FT   DOMAIN          107..330
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   338 AA;  38676 MW;  6C0079D809CE1898 CRC64;
     MRILPQEPVI REEQNWLTIL KNAISDPKLL LKALNLPEDD FEQSIAARKL FSLRVPQPFI
     DKIEKGNPQD PLFLQVMCSD LEFVQAEGFS TDPLEEKNAN AVPNILHKYR NRLLFMAKGG
     CAVNCRYCFR RHFPYDENPG NKKSWQLALD YIAAHSEIEE VIFSGGDPLM AKDHELAWLI
     KHLENIPHLQ RLRIHTRLPV VIPQRITDEF CTLLAETRLQ TVMVTHINHP NEIDQIFAHA
     MQKLNAVNVT LLNQSVLLKG VNDDAQILKI LSDKLFQTGI LPYYLHLLDK VQGASHFLIS
     DIEAMQIYKT LQSLTSGYLV PKLAREIAGE PNKTLYAE