ID A0A1Q2HR83_9BACT Unreviewed; 437 AA.
AC A0A1Q2HR83;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=L-lysine 2,3-aminomutase {ECO:0000256|ARBA:ARBA00022363};
DE EC=5.4.3.2 {ECO:0000256|ARBA:ARBA00012144};
GN Name=kamA {ECO:0000313|EMBL:AQQ09756.1};
GN ORFNames=L21SP3_01568 {ECO:0000313|EMBL:AQQ09756.1};
OS Sedimentisphaera cyanobacteriorum.
OC Bacteria; Planctomycetota; Phycisphaerae; Sedimentisphaerales;
OC Sedimentisphaeraceae; Sedimentisphaera.
OX NCBI_TaxID=1940790 {ECO:0000313|EMBL:AQQ09756.1, ECO:0000313|Proteomes:UP000188273};
RN [1] {ECO:0000313|Proteomes:UP000188273}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L21-RPul-D3 {ECO:0000313|Proteomes:UP000188273};
RA Spring S., Bunk B., Sproer C., Klenk H.-P.;
RT "Comparative genomics and description of representatives of a novel lineage
RT of planctomycetes thriving in anoxic sediments.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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; CP019633; AQQ09756.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2HR83; -.
DR STRING; 1940790.L21SP3_01568; -.
DR KEGG; pbu:L21SP3_01568; -.
DR OrthoDB; 9768064at2; -.
DR Proteomes; UP000188273; 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:SF0; L-LYSINE 2,3-AMINOMUTASE AQ_1632-RELATED; 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; SFLDF00283; L-lysine_2_3-aminomutase_(LAM; 1.
DR SFLD; SFLDS00029; Radical_SAM; 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:0000313|EMBL:AQQ09756.1};
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 120..331
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 134
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 138
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 141
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 346
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603739-50"
SQ SEQUENCE 437 AA; 50353 MW; 609585D1F7F2529A CRC64;
MKLTTNQRQI FDNIDSDAAL SKWQDWKWQI KHCVHDLKTF ENLLEVKLPE EVHEQFKKTV
KKFPMSITPY YLSLINTDDI LNDPIFMQGF PSGKELDIDE YDMEDPLHED NDSPMECITH
RYPDRVLFMV SNTCSMYCRH CTRKRRVGDK DSIPNKKELL AGIEYIKNHP QIRDVLLSGG
DPFLLSDKMI DWLLTELRAI DSVEIIRIGT RTPVVLPQRI TPELVEILKK HQPVWINTHF
NHPREITSSS RRALRLMADA GFPLGNQSVL LAGVNDCPRI MRALVHKLAY NRVRPYYLYQ
CDLSEGLSHF RTPVGKGIEI IESLIGHTSG FCVPTYVIDA PGGGGKIPVM PNYLISWSTN
KVVLRNYEGV ITTYNEPNSY EPSFCDRKCE KCNLQLSLDD ADEYKSLGIS KLLGDYDETI
SLVPENNSRH ERRDSYQ
//
