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Database: UniProt
Entry: A0A1G6M807_9BACL
LinkDB: A0A1G6M807_9BACL
Original site: A0A1G6M807_9BACL 
ID   A0A1G6M807_9BACL        Unreviewed;       435 AA.
AC   A0A1G6M807;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=L-lysine 2,3-aminomutase {ECO:0000256|ARBA:ARBA00022363};
DE            EC=5.4.3.2 {ECO:0000256|ARBA:ARBA00012144};
GN   ORFNames=SAMN04488112_10946 {ECO:0000313|EMBL:SDC51444.1};
OS   Melghirimyces thermohalophilus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC   Melghirimyces.
OX   NCBI_TaxID=1236220 {ECO:0000313|EMBL:SDC51444.1, ECO:0000313|Proteomes:UP000199387};
RN   [1] {ECO:0000313|EMBL:SDC51444.1, ECO:0000313|Proteomes:UP000199387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45514 {ECO:0000313|EMBL:SDC51444.1,
RC   ECO:0000313|Proteomes:UP000199387};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysine = (3S)-3,6-diaminohexanoate; Xref=Rhea:RHEA:19177,
CC         ChEBI:CHEBI:32551, ChEBI:CHEBI:57434; EC=5.4.3.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000911};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR603739-50};
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. KamA family.
CC       {ECO:0000256|ARBA:ARBA00008703}.
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DR   EMBL; FMZA01000009; SDC51444.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6M807; -.
DR   STRING; 1236220.SAMN04488112_10946; -.
DR   OrthoDB; 9768064at2; -.
DR   Proteomes; UP000199387; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0050066; F:lysine 2,3-aminomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd01335; Radical_SAM; 1.
DR   Gene3D; 6.10.140.1170; -; 1.
DR   Gene3D; 6.20.120.40; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR025895; LAM_C_dom.
DR   InterPro; IPR003739; Lys_aminomutase/Glu_NH3_mut.
DR   InterPro; IPR022459; Lysine_aminomutase.
DR   InterPro; IPR007197; rSAM.
DR   NCBIfam; TIGR00238; KamA family radical SAM protein; 1.
DR   NCBIfam; TIGR03820; lys_2_3_AblA; 1.
DR   PANTHER; PTHR30538:SF1; L-LYSINE 2,3-AMINOMUTASE; 1.
DR   PANTHER; PTHR30538; LYSINE 2,3-AMINOMUTASE-RELATED; 1.
DR   Pfam; PF12544; LAM_C; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   PIRSF; PIRSF004911; DUF160; 1.
DR   SFLD; SFLDF00283; L-lysine_2_3-aminomutase_(LAM; 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 {ECO:0000256|PIRSR:PIRSR004911-1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR004911-
KW   1}; Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR004911-1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603739-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199387};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          113..325
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   REGION          413..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         127
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004911-1"
FT   BINDING         131
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004911-1"
FT   BINDING         134
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004911-1"
FT   MOD_RES         339
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603739-50"
SQ   SEQUENCE   435 AA;  50000 MW;  FD12F9CA50318685 CRC64;
     MVRDWREIEL WKDVTEEQWN DWLWQLTHTI RNLEDLKKVV NLKEDEIGGV GISNRTIPLN
     ITPYYALQMD PEDPSCPIRM QSVPLSRELE QTPYDMEDPL LEDTDSPVPG LTHRYPDRVL
     FLITNQCSMY CRYCTRRRFS GQIGMGVGRP QMDACIDYIR NTPEVRDVLL SGGDGLLVND
     RVLEYVLKHL REIPHVEIIR IGTRAPVVFP QRITENLCKI LRKYHPVWLN THFNHPKELT
     PEARRACEML ADAGVPLGNQ AVILAGINDC PHVMKKLNHE LVKTRVRPYY IYQCDLSEGI
     SHFRAPVSKG LEIMEYLRGH TSGYAVPTFV VDAPGGGGKI PVAPNYVISQ SSQKTVLRNF
     EGVITTYPEP DHYQEHDSEN CEYCQAAEGK NVGLASLMAD ERINLEPKVL SREERRGDFE
     RKKRRIREKP PITKS
//
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