Y454_AQUAE
ID Y454_AQUAE Reviewed; 370 AA.
AC O66761;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Putative L-lysine 2,3-aminomutase aq_454;
DE Short=LAM;
DE EC=5.4.3.-;
GN OrderedLocusNames=aq_454;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. KamA family.
CC {ECO:0000305}.
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DR EMBL; AE000657; AAC06722.1; -; Genomic_DNA.
DR PIR; E70341; E70341.
DR RefSeq; NP_213321.1; NC_000918.1.
DR RefSeq; WP_010880259.1; NC_000918.1.
DR AlphaFoldDB; O66761; -.
DR SMR; O66761; -.
DR STRING; 224324.aq_454; -.
DR EnsemblBacteria; AAC06722; AAC06722; aq_454.
DR KEGG; aae:aq_454; -.
DR PATRIC; fig|224324.8.peg.377; -.
DR eggNOG; COG1509; Bacteria.
DR HOGENOM; CLU_032161_0_0_0; -.
DR InParanoid; O66761; -.
DR OMA; PIWLNTH; -.
DR OrthoDB; 557227at2; -.
DR Proteomes; UP000000798; Chromosome.
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 Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR025895; LAM_C_dom.
DR InterPro; IPR003739; Lys_aminomutase/Glu_NH3_mut.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR30538; PTHR30538; 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 TIGRFAMs; TIGR00238; TIGR00238; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Isomerase; Metal-binding; Pyridoxal phosphate;
KW Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..370
FT /note="Putative L-lysine 2,3-aminomutase aq_454"
FT /id="PRO_0000172290"
FT DOMAIN 107..322
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 121
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255"
FT BINDING 125
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255"
FT BINDING 128
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255"
FT MOD_RES 334
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 370 AA; 43494 MW; BA7B8CFB54949E5E CRC64;
MRRFFENVPE NLWRSYEWQI QNRIKTLKEI KKYLKLLPEE EEGIKRTQGL YPFAITPYYL
SLINPEDPKD PIRLQAIPRV VEVDEKVQSA GEPDALKEEG DIPGLTHRYP DRVLLNVTTF
CAVYCRHCMR KRIFSQGERA RTKEEIDTMI DYIKRHEEIR DVLISGGEPL SLSLEKLEYL
LSRLREIKHV EIIRFGTRLP VLAPQRFFND KLLDILEKYS PIWINTHFNH PNEITEYAEE
AVDRLLRRGI PVNNQTVLLK GVNDDPEVML KLFRKLLRIK VKPQYLFHCD PIKGAVHFRT
TIDKGLEIMR YLRGRLSGFG IPTYAVDLPG GKGKVPLLPN YVKKRKGNKF WFESFTGEVV
EYEVTEVWEP
