ID A0A1F8KJF6_9CHLR Unreviewed; 443 AA.
AC A0A1F8KJF6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=L-lysine 2,3-aminomutase {ECO:0000256|ARBA:ARBA00022363};
DE EC=5.4.3.2 {ECO:0000256|ARBA:ARBA00012144};
GN ORFNames=A2X25_06420 {ECO:0000313|EMBL:OGN74513.1};
OS Chloroflexi bacterium GWB2_49_20.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797612 {ECO:0000313|EMBL:OGN74513.1, ECO:0000313|Proteomes:UP000178842};
RN [1] {ECO:0000313|EMBL:OGN74513.1, ECO:0000313|Proteomes:UP000178842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGN74513.1}.
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DR EMBL; MGMF01000014; OGN74513.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8KJF6; -.
DR STRING; 1797612.A2X25_06420; -.
DR Proteomes; UP000178842; 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 S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 114..326
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 128
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 132
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 135
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 340
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603739-50"
SQ SEQUENCE 443 AA; 50493 MW; 407B70E3161DD241 CRC64;
MPLPFTSRRA PFYADIPDEK WNDWRWQLSH RLNTVEEIEK VITLTDSERK ALNASGLFRV
EVTPYFISLI RPEDPNDPIR KQIIPTASEM VSFTSMMEDS LAEDRHSPVP GLVHRYPDRV
LMLVTTQCAS YCRYCTRSRI VGDPTATFSR NEFEMQIDYI KRTPQVRDVL LSGGDPLVLA
PKILEEILTR LREIPHVEIV RIGSRVPVFL PMRVTQELCD MLEKFHPLWL NIHVNHPNEI
SQELADATNR MAKAGIPLGN QSVLLAGVND CVHIQRKLVH DLVRIRVRPY YLYQADLVEG
GGHFRTAVAK GIEIIEGLRG HTSGYAVPQF IVDAPGGGGK IPLMPNYLLS YSDHKVVVRN
YEGYVTTYEE PLDYKPHDPK TCSFCQNKRL EPGQTGITGL LDGDHMFIKP KDFDEVHDRH
GIQHRLKDES KWKPLGIGDG TEV
//
