ID E1RFJ3_METP4 Unreviewed; 437 AA.
AC E1RFJ3;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=L-lysine 2,3-aminomutase {ECO:0000256|ARBA:ARBA00022363};
DE EC=5.4.3.2 {ECO:0000256|ARBA:ARBA00012144};
GN OrderedLocusNames=Mpet_1464 {ECO:0000313|EMBL:ADN36223.1};
OS Methanolacinia petrolearia (strain DSM 11571 / OCM 486 / SEBR 4847)
OS (Methanoplanus petrolearius).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanolacinia.
OX NCBI_TaxID=679926 {ECO:0000313|EMBL:ADN36223.1, ECO:0000313|Proteomes:UP000006565};
RN [1] {ECO:0000313|EMBL:ADN36223.1, ECO:0000313|Proteomes:UP000006565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11571 / OCM 486 / SEBR 4847
RC {ECO:0000313|Proteomes:UP000006565};
RX PubMed=21304750;
RA Brambilla E., Djao O.D., Daligault H., Lapidus A., Lucas S., Hammon N.,
RA Nolan M., Tice H., Cheng J.F., Han C., Tapia R., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA Spring S., Sikorski J., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Methanoplanus petrolearius type strain (SEBR
RT 4847).";
RL Stand. Genomic Sci. 3:203-211(2010).
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; CP002117; ADN36223.1; -; Genomic_DNA.
DR RefSeq; WP_013329400.1; NC_014507.1.
DR AlphaFoldDB; E1RFJ3; -.
DR STRING; 679926.Mpet_1464; -.
DR GeneID; 9743934; -.
DR KEGG; mpi:Mpet_1464; -.
DR eggNOG; arCOG03246; Archaea.
DR HOGENOM; CLU_032161_0_0_2; -.
DR OrthoDB; 21308at2157; -.
DR Proteomes; UP000006565; 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; 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, ECO:0000313|EMBL:ADN36223.1};
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:UP000006565};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 121..333
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
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 BINDING 139
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 142
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 347
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603739-50"
SQ SEQUENCE 437 AA; 50557 MW; A2029CAD7DAAD17B CRC64;
MINYSDTQKE ITLKIDSEGT LSKWRDWRWQ LSHTIRDLDT FEKITGITFT NEKYEELKET
LEKFPLAITP YYLSLIETED YENDPIFMQS FPSVHELDII EEDLADPLDE DRDSPVEGIT
HRYPDRVLFL VSNKCAMYCR HCTRKRKVGD VEYIPDKDQI SKGIDYINNN PQVRDVLLSG
GDPLLLDDSY LEWILSELTE IPHVEIVRIG SRLPVVLPYR IDSNLVEMLR QYHPIWFNTQ
FNHPREITSS STEALRKLAD GGIPLGNQSV LLSGVNDCPR IMKTLMHKLV MNRVRPYYMY
QCDLSEGLSH FRTPVGKGIE IIESLRGHTS GFAVPTYVID APGGGGKIPL MPNYLISWST
NKVVLRNYEG VICTYKEPDN YEAVYCNRKC EECTLQLKLD NADESKSIGI EKLLCDYDDT
IALYPENNER MERRDEK
//