ID A0A0G1FWE3_9BACT Unreviewed; 382 AA.
AC A0A0G1FWE3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 22.
DE SubName: Full=Lysine 2,3-aminomutase {ECO:0000313|EMBL:KKT26786.1};
GN ORFNames=UW11_C0006G0052 {ECO:0000313|EMBL:KKT26786.1};
OS Parcubacteria group bacterium GW2011_GWA2_43_9b.
OC Bacteria.
OX NCBI_TaxID=1618828 {ECO:0000313|EMBL:KKT26786.1, ECO:0000313|Proteomes:UP000034814};
RN [1] {ECO:0000313|EMBL:KKT26786.1, ECO:0000313|Proteomes:UP000034814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR603739-50};
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:KKT26786.1}.
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DR EMBL; LCHB01000006; KKT26786.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1FWE3; -.
DR STRING; 1618828.UW11_C0006G0052; -.
DR PATRIC; fig|1618828.3.peg.256; -.
DR Proteomes; UP000034814; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR025895; LAM_C_dom.
DR InterPro; IPR003739; Lys_aminomutase/Glu_NH3_mut.
DR InterPro; IPR007197; rSAM.
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; PF13353; Fer4_12; 1.
DR Pfam; PF12544; LAM_C; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF004911; DUF160; 1.
DR SFLD; SFLDG01070; PLP-dependent; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 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};
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 122..332
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 136
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 140
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 143
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 382 AA; 43910 MW; DC689F10C0043A9C CRC64;
MCNKFGILLI IVSSFSFDTL INNDNLITLW QNQLKMGISS INKLRVAFER AGIKKPAKFY
RELAKVTKSY PIFISPSIFK QCLKSKSIYR QFIPDEKELI NFRGENDPLK EDNKKATDKL
IHMYPDRALL LATDMCFSSC RFCTRKRIKK LCERITLKQL DDACKYIAKN KQIKDVIISG
GDPLTIEDSC LKTILERIKK IKSVKVIRIG TRAPVSCPDR ITDRLVKLLK KFNPLYINVH
LNHPDEFTPA TVKALRKLSD AGIILGSQSV LLKGVNDNNK IIKELLYKCI ETGVRPYYLY
QCDEVLGTEH FWTEYQEMFK IADNLIGNIS GLATPSFVFD CKGGQGKVRV IPEFYKSKKE
KSITLKTFKN KLYTYNNLSK KK
//
