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Database: UniProt
Entry: A0A0Q6ASM6_9BRAD
LinkDB: A0A0Q6ASM6_9BRAD
Original site: A0A0Q6ASM6_9BRAD 
ID   A0A0Q6ASM6_9BRAD        Unreviewed;       364 AA.
AC   A0A0Q6ASM6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Lysine 2,3-aminomutase {ECO:0000313|EMBL:KQT29353.1};
GN   ORFNames=ASG57_01605 {ECO:0000313|EMBL:KQT29353.1};
OS   Bradyrhizobium sp. Leaf396.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1736363 {ECO:0000313|EMBL:KQT29353.1, ECO:0000313|Proteomes:UP000051536};
RN   [1] {ECO:0000313|EMBL:KQT29353.1, ECO:0000313|Proteomes:UP000051536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf396 {ECO:0000313|EMBL:KQT29353.1,
RC   ECO:0000313|Proteomes:UP000051536};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQT29353.1, ECO:0000313|Proteomes:UP000051536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf396 {ECO:0000313|EMBL:KQT29353.1,
RC   ECO:0000313|Proteomes:UP000051536};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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   -!- 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:KQT29353.1}.
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DR   EMBL; LMQJ01000001; KQT29353.1; -; Genomic_DNA.
DR   RefSeq; WP_024337829.1; NZ_LMQJ01000001.1.
DR   AlphaFoldDB; A0A0Q6ASM6; -.
DR   OrthoDB; 9768064at2; -.
DR   Proteomes; UP000051536; 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; IPR025895; LAM_C_dom.
DR   InterPro; IPR022447; Lys_aminomutase-rel.
DR   InterPro; IPR003739; Lys_aminomutase/Glu_NH3_mut.
DR   InterPro; IPR007197; rSAM.
DR   NCBIfam; TIGR03822; AblA_like_2; 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; 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   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          93..306
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   BINDING         107
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         111
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         114
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         321
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603739-50"
SQ   SEQUENCE   364 AA;  39469 MW;  983626D19E4D034F CRC64;
     MTKANLARTL REPAELIAEG LAPAAALPAL ERVAARYAVA VTPDLAELID ASDPDDPIAR
     QFVPTAAELD LKPGENADPI GDHPHSPVPG IVHRYPDRVL FKLVHVCAVY CRFCFRREMV
     GPGKENALSD SAYRAAIDYI RAHDEIWEVI LTGGDPLMLS PRRMSEIMAD LAAIQHVKII
     RLHSRVPVAE PARISDEMVA ALKVDGATTW IALHANHARE LTGAARAACA RLVDAGVPMV
     SQSVLLRGVN DNIVALSDLM RAFVECRIKP YYLHHGDLAP GTAHLRTTLA QGQDLMRQLR
     GRVSGLCQPD YVIDIPGGAG KSPVGPSYLL TTQNTALPAD DAGAETRYRI VDYCGDVHLY
     PPET
//
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