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 27-MAR-2024, entry version 117.
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; Pseudomonadota; 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 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 OrthoDB; 9770937at2; -.
DR PhylomeDB; P44641; -.
DR BioCyc; HINF71421:G1GJ1-345-MONOMER; -.
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 CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR022462; EpmB.
DR InterPro; IPR003739; Lys_aminomutase/Glu_NH3_mut.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR03821; EFP_modif_epmB; 1.
DR NCBIfam; TIGR00238; KamA family radical SAM protein; 1.
DR PANTHER; PTHR30538:SF1; L-LYSINE 2,3-AMINOMUTASE; 1.
DR PANTHER; PTHR30538; LYSINE 2,3-AMINOMUTASE-RELATED; 1.
DR Pfam; PF13353; Fer4_12; 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 SUPFAM; SSF102114; Radical SAM enzymes; 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
//
