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
//