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Database: UniProt
Entry: D5X7U1_THEPJ
LinkDB: D5X7U1_THEPJ
Original site: D5X7U1_THEPJ 
ID   D5X7U1_THEPJ            Unreviewed;       448 AA.
AC   D5X7U1;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Lysine 2,3-aminomutase YodO family protein {ECO:0000313|EMBL:ADG82661.1};
DE            EC=5.4.3.2 {ECO:0000313|EMBL:ADG82661.1};
GN   OrderedLocusNames=TherJR_1812 {ECO:0000313|EMBL:ADG82661.1};
OS   Thermincola potens (strain JR).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Thermincolaceae;
OC   Thermincola.
OX   NCBI_TaxID=635013 {ECO:0000313|EMBL:ADG82661.1, ECO:0000313|Proteomes:UP000002377};
RN   [1] {ECO:0000313|EMBL:ADG82661.1, ECO:0000313|Proteomes:UP000002377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JR {ECO:0000313|EMBL:ADG82661.1,
RC   ECO:0000313|Proteomes:UP000002377};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Hazen T.C., Woyke T.;
RT   "Complete sequence of Thermincola sp. JR.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR603739-50};
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DR   EMBL; CP002028; ADG82661.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5X7U1; -.
DR   STRING; 635013.TherJR_1812; -.
DR   KEGG; tjr:TherJR_1812; -.
DR   eggNOG; COG1509; Bacteria.
DR   HOGENOM; CLU_032161_0_1_9; -.
DR   Proteomes; UP000002377; Chromosome.
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; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR030801; Glu_2_3_NH3_mut.
DR   InterPro; IPR025895; LAM_C_dom.
DR   InterPro; IPR003739; Lys_aminomutase/Glu_NH3_mut.
DR   InterPro; IPR007197; rSAM.
DR   NCBIfam; TIGR04368; Glu_2_3_NH3_mut; 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; PF12544; LAM_C; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   PIRSF; PIRSF004911; DUF160; 2.
DR   SFLD; SFLDF00290; glutamate_2_3-aminomutase; 1.
DR   SFLD; SFLDG01070; PLP-dependent; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   4: Predicted;
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, ECO:0000313|EMBL:ADG82661.1};
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:UP000002377};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          178..399
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   BINDING         192
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         196
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         199
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         404
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603739-50"
SQ   SEQUENCE   448 AA;  51634 MW;  B2C436C4918A479A CRC64;
     MVMKEDYMLH QEVENSSAKN DQVQRIITPE EKRQVALERA AELKLRIEDY LVARDHIETG
     FDQWPRIEKR KARILQVLNG TEADWNDWKW HMKNRIRDVE VLAQIIDLTD KEIEDIKKVG
     QKFRWAISPY YASLMSERDP SCPVRLQAIP SILELLDQSG KDDPMGEEFT SPAPCITRRY
     PDRLIINVTN QCAMYCRHCQ RRRNIGEVDR NKPRSEIKAA IEYIRANPEI RDVLITGGDA
     LLLSNSELDW ILTQLDSIPH VEIKRIGTRT LVSMPQRITP QLCEILEKHP PLYINTQFNH
     PKEITPAVAE ACDKLIKAGA VLGNQAVLLN GINNNVHVMK KLNHELLKVR IRPYYIFHAK
     TVTGTSHFIT KVEEGIKIME KLRGYTSGLA VPTYIINAPK GYGKTPMLPE YLISSGEDEI
     VIRTWEKKVI SYPNKKHFKT DLNLVKST
//
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