ID A0A0F3GQ39_9BACT Unreviewed; 433 AA.
AC A0A0F3GQ39;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Lysine 2,3-aminomutase YodO family protein {ECO:0000313|EMBL:KJU84050.1};
GN ORFNames=MBAV_003755 {ECO:0000313|EMBL:KJU84050.1};
OS Candidatus Magnetobacterium bavaricum.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Magnetobacterium.
OX NCBI_TaxID=29290 {ECO:0000313|EMBL:KJU84050.1, ECO:0000313|Proteomes:UP000033423};
RN [1] {ECO:0000313|EMBL:KJU84050.1, ECO:0000313|Proteomes:UP000033423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM-1 {ECO:0000313|EMBL:KJU84050.1};
RA Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.;
RT "Single-cell genomics of uncultivated deep-branching MTB reveals a
RT conserved set of magnetosome genes.";
RL Submitted (FEB-2015) 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};
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:KJU84050.1}.
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DR EMBL; LACI01001636; KJU84050.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F3GQ39; -.
DR PATRIC; fig|29290.4.peg.4997; -.
DR Proteomes; UP000033423; 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; 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; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000033423};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 136..347
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 150
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 154
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 157
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 362
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603739-50"
SQ SEQUENCE 433 AA; 49674 MW; DCC6A59BB4C2D009 CRC64;
MLKVYNKSCR GTMENDCLLK EEEPPAQGIL RRFWPDVTSR QWNDWRWQQS NSLRSVQALR
ELLNLSTHEV LRYEELTRRF HYCITPYYLS LIDFTNPDDP IRKQSIPDIS ELDFQRVGHS
DPLEEGEDTQ VPGLVHRYPD RALAVVTSRC AMYCRHCTRK RMWHEGESFR TRQELAAMVD
YIRGEPGIRE VIVSGGDPLT MNLRLLDWFL GELRTAPSLE VIRIGTRMPV VMPMGITDDL
VRMLARHRPL WLNTQFNHPA ELTPASIEAC DKILRAGIPV SNQSVLLRGV NDSVEVMKEL
CHALQRIMVR PYYLFQCDPV IGVEHFRTSI WKGIEIIEMM RGHTGGLCIP SFVVDAPGGG
GKVPLQPFYL LSASEDEVLL RNYEGTIIRY YNPGRSLTEA GQESGAQQTH RILAGTDITA
RYKRRRSKAA LAH
//