ID D2R4K4_PIRSD Unreviewed; 370 AA.
AC D2R4K4;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
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 OrderedLocusNames=Psta_2400 {ECO:0000313|EMBL:ADB17070.1};
OS Pirellula staleyi (strain ATCC 27377 / DSM 6068 / ICPB 4128) (Pirella
OS staleyi).
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Pirellula.
OX NCBI_TaxID=530564 {ECO:0000313|EMBL:ADB17070.1, ECO:0000313|Proteomes:UP000001887};
RN [1] {ECO:0000313|EMBL:ADB17070.1, ECO:0000313|Proteomes:UP000001887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27377 / DSM 6068 / ICPB 4128
RC {ECO:0000313|Proteomes:UP000001887};
RX PubMed=21304671; DOI=10.4056/sigs.51657;
RA Clum A., Tindall B.J., Sikorski J., Ivanova N., Mavrommatis K., Lucas S.,
RA Glavina del Rio T., Nolan M., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA Goodwin L., Ovchinikova G., Pati A., Mikhailova N., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Pirellula staleyi type strain (ATCC 27377).";
RL Stand. Genomic Sci. 1:308-316(2009).
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=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; CP001848; ADB17070.1; -; Genomic_DNA.
DR RefSeq; WP_012911332.1; NC_013720.1.
DR AlphaFoldDB; D2R4K4; -.
DR STRING; 530564.Psta_2400; -.
DR KEGG; psl:Psta_2400; -.
DR eggNOG; COG1509; Bacteria.
DR HOGENOM; CLU_032161_2_0_0; -.
DR OrthoDB; 9768064at2; -.
DR Proteomes; UP000001887; Chromosome.
DR GO; GO:0051536; F:iron-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 SFLD; SFLDF00314; L-lysine_2_3-aminomutase_(yjeK; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ADB17070.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603739-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000001887};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 141..353
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 367
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603739-50"
SQ SEQUENCE 370 AA; 40387 MW; A844257231F80AB7 CRC64;
MQIVAGNREN VRSSSPGESS GGQGSIISAS DWRKTLRESL RTLPELLEAV GLTKSPEHLA
ATSIAGPSGA IDPAFVPLDA AAEQFRVLVP GPYLSRIERG NPADPLLLQV LPVAGEMSSP
ADFLTDPVGD RESERLPGLL QKYDGRALMI LSGSCAVHCR YCFRRHYPYD ETPRGLAGWQ
PAIDEIAADE SVQEVILSGG DPLTIVDSTL AELAHRFAEI PHLKRLRVHS RVPVVIPERV
NDELIGWMRG TRLAPYMVVH INHPREIDSA VAAALARLVD AGIVVMNQAV LLRGVNDNFE
ALHELCETLV NMRVLPYYLS QLDRVAGAAH FLVEESRGRE LIEQLRASLP GYAIPRYVAE
IPGRSSKSPL
//
