Y1632_AQUAE
ID Y1632_AQUAE Reviewed; 374 AA.
AC O67554;
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_1632;
DE Short=LAM;
DE EC=5.4.3.-;
GN OrderedLocusNames=aq_1632;
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}.
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; AE000657; AAC07521.1; -; Genomic_DNA.
DR PIR; H70440; H70440.
DR RefSeq; NP_214119.1; NC_000918.1.
DR RefSeq; WP_010881057.1; NC_000918.1.
DR AlphaFoldDB; O67554; -.
DR SMR; O67554; -.
DR STRING; 224324.aq_1632; -.
DR PRIDE; O67554; -.
DR EnsemblBacteria; AAC07521; AAC07521; aq_1632.
DR KEGG; aae:aq_1632; -.
DR PATRIC; fig|224324.8.peg.1259; -.
DR eggNOG; COG1509; Bacteria.
DR HOGENOM; CLU_032161_3_1_0; -.
DR InParanoid; O67554; -.
DR OMA; WAQFVGD; -.
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; IPR003739; Lys_aminomutase/Glu_NH3_mut.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR30538; PTHR30538; 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..374
FT /note="Putative L-lysine 2,3-aminomutase aq_1632"
FT /id="PRO_0000172291"
FT DOMAIN 86..314
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 100
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255"
FT BINDING 104
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255"
FT BINDING 107
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 317
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 374 AA; 43371 MW; 5ADF6FFA1B9A88CB CRC64;
MGKKLKYIID LKFIEEIPEE ERRELEKVTE KFAFRTNTYY NSLINWDNPN DPIRRIVIPT
TEELEVWGKL DASNESKYMK VHGLEHKYPD TALLLVTDVC GIYCRFCFRK RLFMNDNDEV
ARDVSEGLEY IRNHPEINNV LLTGGDPLIL ATFKLEKILK ALAEIPHVRI VRIGSKMLAV
NPFRVLDDPK LLELFEWFNT ETGKKLYLMN HFNHPRELTK EARKAVELVQ KTGTTLTNQT
PILKGINDDF ETLKTLLEEL SFIGVPPYYV FQCRPTAGNK AYSTPIEETI DLVEAVRAEV
SGLAARVRYV MSHETGKIEI LGKTDEHIFF RYHRAADPEN RGKFMVFKRN PEAHWFDDYT
ELVAEYKSSL SGVS