ID A0A097QYB7_HAFAL Unreviewed; 344 AA.
AC A0A097QYB7;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=L-lysine 2,3-aminomutase {ECO:0000256|ARBA:ARBA00022363};
DE AltName: Full=EF-P post-translational modification enzyme B {ECO:0000256|ARBA:ARBA00030756};
GN ORFNames=AT03_03070 {ECO:0000313|EMBL:AIU71469.1};
OS Hafnia alvei FB1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Hafnia.
OX NCBI_TaxID=1453496 {ECO:0000313|EMBL:AIU71469.1, ECO:0000313|Proteomes:UP000029986};
RN [1] {ECO:0000313|EMBL:AIU71469.1, ECO:0000313|Proteomes:UP000029986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB1 {ECO:0000313|EMBL:AIU71469.1,
RC ECO:0000313|Proteomes:UP000029986};
RX PubMed=25075225; DOI=10.1186/1757-4749-6-29;
RA Tan J.Y., Yin W.F., Chan K.G.;
RT "Gene clusters of Hafnia alvei strain FB1 important in survival and
RT pathogenesis: a draft genome perspective.";
RL Gut Pathog. 6:29-29(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysine = D-beta-lysine; Xref=Rhea:RHEA:44148,
CC ChEBI:CHEBI:32551, ChEBI:CHEBI:84138;
CC Evidence={ECO:0000256|ARBA:ARBA00001352};
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; CP009706; AIU71469.1; -; Genomic_DNA.
DR RefSeq; WP_025798717.1; NZ_CP009706.1.
DR AlphaFoldDB; A0A097QYB7; -.
DR KEGG; hav:AT03_03070; -.
DR PATRIC; fig|1453496.5.peg.609; -.
DR eggNOG; COG1509; Bacteria.
DR HOGENOM; CLU_032161_2_0_6; -.
DR OrthoDB; 9770937at2; -.
DR Proteomes; UP000029986; 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 CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR022462; EpmB.
DR InterPro; IPR003739; Lys_aminomutase/Glu_NH3_mut.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR03821; EFP_modif_epmB; 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; PF13353; Fer4_12; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF004911; DUF160; 1.
DR SFLD; SFLDF00314; L-lysine_2_3-aminomutase_(yjeK; 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};
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:UP000029986};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 108..323
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 122
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 126
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 129
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 334
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603739-50"
SQ SEQUENCE 344 AA; 39155 MW; DE72F0695110266B CRC64;
MAHIVTQNTQ SREDWLQQLA DVITEPAELL EYLALSDSPE WQKGHDARRL FALRVPHAFA
RRMKKGDPND PLLLQVMTSA NEFIATPGYS TDPLEEQDDA IAVPGLLHKY INRALLLVKG
GCAVNCRYCF RRHFPYQENQ GNKANWRHAL DYIRQQPELD EIIFSGGDPL MAKDHELAWL
LDEIETIPHI KRLRIHSRLP VVIPARITEA LTQRFSQSRL QILLVTHVNH ANEIDSEFCD
AMTRLKRANV TLLNQGVLLR GVNDNADTLA NLSNALFDAG IMPYYLHVLD RVQGAAHFMV
PDDEARLIMR ELMTKVSGYM VPKLTREIGG EPSKTTIDLG LRQR
//
