ID Q5FUC9_GLUOX Unreviewed; 356 AA.
AC Q5FUC9;
DT 01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Lysine 2,3-aminomutase {ECO:0000313|EMBL:AAW60017.1};
DE EC=5.4.3.2 {ECO:0000313|EMBL:AAW60017.1};
GN OrderedLocusNames=GOX0234 {ECO:0000313|EMBL:AAW60017.1};
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633 {ECO:0000313|EMBL:AAW60017.1, ECO:0000313|Proteomes:UP000006375};
RN [1] {ECO:0000313|EMBL:AAW60017.1, ECO:0000313|Proteomes:UP000006375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H {ECO:0000313|EMBL:AAW60017.1,
RC ECO:0000313|Proteomes:UP000006375};
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(2005).
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};
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DR EMBL; CP000009; AAW60017.1; -; Genomic_DNA.
DR RefSeq; WP_011251820.1; NZ_LT900338.1.
DR AlphaFoldDB; Q5FUC9; -.
DR STRING; 290633.GOX0234; -.
DR KEGG; gox:GOX0234; -.
DR eggNOG; COG1509; Bacteria.
DR HOGENOM; CLU_032161_2_0_5; -.
DR Proteomes; UP000006375; 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; 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; 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, ECO:0000313|EMBL:AAW60017.1};
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:UP000006375};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 103..318
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 117
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 121
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 124
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 329
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603739-50"
SQ SEQUENCE 356 AA; 38815 MW; F519640A72704DC8 CRC64;
MDDMVKTASQ HSAGPSAKRH TLRTPSDLID AGLATEADRA TLEAVGERFT MAIPPAFRDL
ITHPDDPIAR QVIPDARELV TLPHEDPDPI GDDALSPVPG IVHRYADRAL LKPLLVCPLY
CRFCFRREHV GPGGGLLSNA QLETALDWVR QHPDIREIIL TGGDPLMLAP RRLKHIVQSL
SGIPHIETIR IHSRVPVADP ARMTEELLDA METDRAMWLV IHANHASELT PHATKAIRAV
LSRAIPVLSQ SVLLRGVNDT VESLEALLRA LIKARVKPYY LHHLDAAAGT GHFHVPVAQG
QALLRQLRGR VTGLAWPTYV LDIPSGRGKV PIGPEYLDPA SPGTVSTPDG EACSFT
//
