ID A0A6L8PIM4_BACAN Unreviewed; 473 AA. AC A0A6L8PIM4; A0A1S0QKI9; E9R2D8; E9R2D9; Q6HZ32; Q6KT31; Q81QW5; DT 07-OCT-2020, integrated into UniProtKB/TrEMBL. DT 07-OCT-2020, sequence version 1. DT 27-MAR-2024, entry version 16. 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:AAT31423.1}; GN OrderedLocusNames=GBAA_2300 {ECO:0000313|EMBL:AAT31423.1}; OS Bacillus anthracis. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1392 {ECO:0000313|EMBL:AAT31423.1, ECO:0000313|Proteomes:UP000000594}; RN [1] {ECO:0000313|EMBL:AAT31423.1, ECO:0000313|Proteomes:UP000000594} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ames ancestor {ECO:0000313|Proteomes:UP000000594}; RX PubMed=18952800; DOI=10.1128/JB.01347-08; RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.; RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'."; RL J. Bacteriol. 191:445-446(2009). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE017334; AAT31423.1; -; Genomic_DNA. DR RefSeq; WP_000902136.1; NZ_WXXJ01000017.1. DR AlphaFoldDB; A0A6L8PIM4; -. DR GeneID; 75085477; -. DR KEGG; bar:GBAA_2300; -. DR PATRIC; fig|1392.230.peg.2260; -. DR OMA; CAIHCRY; -. DR OrthoDB; 9768064at2; -. DR Proteomes; UP000000594; Chromosome. DR GO; GO:0051536; F:iron-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; PF13353; Fer4_12; 1. DR Pfam; PF12544; LAM_C; 1. DR Pfam; PF04055; Radical_SAM; 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 Iron {ECO:0000256|ARBA:ARBA00023004}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AAT31423.1}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603739-50}; KW Reference proteome {ECO:0000313|Proteomes:UP000000594}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}. FT DOMAIN 120..332 FT /note="Radical SAM core" FT /evidence="ECO:0000259|PROSITE:PS51918" FT REGION 425..473 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 346 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|PIRSR:PIRSR603739-50" SQ SEQUENCE 473 AA; 54396 MW; FFD049EF33550226 CRC64; MLHDVYKPNR HWKDIELWKD VTEEQWNDWV WQLTNTIKTL DDLKKVINLT PDEEEGVKIS TKTIPLNITP YYAWLMNPDD PRCPIRMQSV PISEELYKTK YDLEDPLHED EDSPVPGLTH RYPDRVLFLV TNQCSMYCRY CTRRRFSGQI GMGVPKKQLD DAIAYIRETP QVRDVLISGG DGLLINDKIL EYVLKNLREI PHVEIIRIGT RAPVVFPQRI TENLCNIIKK YHPVWLNTHF NTSIEITEES KKACEMLANA GVPVGNQAVI LAGINDSVPI MKKLMHDLVK IRVRPYYIYQ CDLSEGIGHF RAPVSKGLEI IEGLRGHTSG YAVPTFVVDA PGGGGKIALQ PNYLISQSAD KVVLRNFEGV ITTYPEPESY IPGRAEGYFK EIYPNYEEKR SDVGIAGLMS DKKFNLVPDD LQRMNRRKDY EDNETHATLK DKRDKRDQLK DKKYQAQMAK LEENDKKTEG DAV //