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Database: UniProt
Entry: A0A1B1Q320_9CHLB
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ID   A0A1B1Q320_9CHLB        Unreviewed;       414 AA.
AC   A0A1B1Q320;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
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:ANT65239.1};
GN   ORFNames=Ptc2401_01487 {ECO:0000313|EMBL:ANT65239.1};
OS   Prosthecochloris sp. CIB 2401.
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC   Prosthecochloris.
OX   NCBI_TaxID=1868325 {ECO:0000313|EMBL:ANT65239.1, ECO:0000313|Proteomes:UP000092496};
RN   [1] {ECO:0000313|EMBL:ANT65239.1, ECO:0000313|Proteomes:UP000092496}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIB 2401 {ECO:0000313|EMBL:ANT65239.1,
RC   ECO:0000313|Proteomes:UP000092496};
RA   Nabhan S., Bunk B., Sproeer C., Bryant D.A., Overmann J.;
RT   "Genome Sequence of Prosthecochloris phaeum CIB2401 of the phylum
RT   Chlorobi.";
RL   Submitted (JUL-2016) 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; CP016432; ANT65239.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B1Q320; -.
DR   STRING; 1868325.Ptc2401_01487; -.
DR   KEGG; proc:Ptc2401_01487; -.
DR   PATRIC; fig|1868325.3.peg.1448; -.
DR   InParanoid; A0A1B1Q320; -.
DR   Proteomes; UP000092496; 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; 6.20.120.40; -; 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; 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; SFLDG01070; PLP-dependent; 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:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ANT65239.1};
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:UP000092496};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          91..302
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   BINDING         105
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         109
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         112
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         317
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603739-50"
SQ   SEQUENCE   414 AA;  46960 MW;  A56E4AA8E7289CE5 CRC64;
     MRHSIRDLAS FEKLLGISLG EEQRTAFEKT VEKFPMSITP YYLSLIDTED MQHDPIFLQS
     VPLPQELDIL KGDMADPLHE DQDSPAPCVT HRYPDRVLLL VSNTCPMYCR HCTRKRRVGD
     KDTIPNKSAI LQGIDYIRNT PQVRDVLLSG GDPFLLSDDY LDWILTELRS IDHVEIIRIG
     TRTPVVLPYR ITPELTAILK KHKPVWVNTH FNHPREITQS ARTALDMLAD AGIPLGNQTV
     LLSGINDCPR IMKALVHQLT RNRVRPYYLY QCDLSEGLSH FRTPVGKGIE ILESLIGHTS
     GFCVPTYVID APGGGGKIPV MPNYLISWST NKVVLRNYEG VITTYKEPDS YEPTFCDRNC
     ESCDLLLKLD NADENKSIGI EQLLSDYDQT ISLIPASNAR HSRRKTEETE ETEE
//
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