EAM_CLOD6
ID EAM_CLOD6 Reviewed; 422 AA.
AC Q185C5;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Glutamate 2,3-aminomutase;
DE EC=5.4.3.9;
GN Name=eam; OrderedLocusNames=CD630_22520;
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=272563;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630;
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX PubMed=17222594; DOI=10.1016/j.bbapap.2006.11.008;
RA Ruzicka F.J., Frey P.A.;
RT "Glutamate 2,3-aminomutase: a new member of the radical SAM superfamily of
RT enzymes.";
RL Biochim. Biophys. Acta 1774:286-296(2007).
CC -!- FUNCTION: Catalyzes the interconversion of L-glutamate and L-beta-
CC glutamate. Does not have L-lysine 2,3-aminomutase activity.
CC {ECO:0000269|PubMed:17222594}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamate = 3-aminopentanedioate; Xref=Rhea:RHEA:34239,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:66948; EC=5.4.3.9;
CC Evidence={ECO:0000269|PubMed:17222594};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:17222594};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01266};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.3 mM for L-glutamate {ECO:0000269|PubMed:17222594};
CC Note=kcat is 6.1 sec(-1) with L-glutamate as substrate.;
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. {ECO:0000305}.
CC -!- CAUTION: Highly similar to the L-lysine 2,3-aminomutase. However lacks
CC lysyl-binding Asp residues at positions 332 and 369, that are replaced
CC by Lys and Asn residues, respectively (PubMed:17222594).
CC {ECO:0000305|PubMed:17222594}.
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DR EMBL; AM180355; CAJ69138.1; -; Genomic_DNA.
DR RefSeq; WP_003430434.1; NZ_CP010905.2.
DR RefSeq; YP_001088767.1; NC_009089.1.
DR AlphaFoldDB; Q185C5; -.
DR SMR; Q185C5; -.
DR STRING; 272563.CD630_22520; -.
DR EnsemblBacteria; CAJ69138; CAJ69138; CD630_22520.
DR KEGG; cdf:CD630_22520; -.
DR KEGG; pdc:CDIF630_02487; -.
DR PATRIC; fig|272563.120.peg.2380; -.
DR eggNOG; COG1509; Bacteria.
DR OMA; VTNQCAM; -.
DR PhylomeDB; Q185C5; -.
DR BioCyc; MetaCyc:G12WB-2408-MON; -.
DR BioCyc; PDIF272563:G12WB-2408-MON; -.
DR Proteomes; UP000001978; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016869; F:intramolecular transferase activity, transferring amino groups; IDA:UniProtKB.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR030801; Glu_2_3_NH3_mut.
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; SFLDF00290; glutamate_2_3-aminomutase; 1.
DR SFLD; SFLDG01070; PLP-dependent; 1.
DR TIGRFAMs; TIGR04368; Glu_2_3_NH3_mut; 1.
DR TIGRFAMs; TIGR00238; TIGR00238; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Isomerase; Metal-binding; Pyridoxal phosphate;
KW Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..422
FT /note="Glutamate 2,3-aminomutase"
FT /id="PRO_0000421754"
FT DOMAIN 150..371
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 164
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT MOD_RES 376
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 422 AA; 48980 MW; 03E49F10A73128F7 CRC64;
MNEQTRISLE RAAELKSKID DYIQARKTIN RGLEKEEEIN KRKQKILSIL NGTEEDWNNY
KWQLSNRITD VDTLSKIITL TKKEKEYIKE VGTQFRWAIS PYYLSLIDPE DICDPIKLLS
IPTHIELEDE QEDLDPMGEE YTNPAGCITR RYPDRLIINV TNECAMYCRH CQRRRNIGQQ
DSHKSKAIIQ ESIDYIRENE EIRDVLVTGG DALTLKDDYL EWILSQLKEI PHVDYVRLGT
RTLVTMPQRI TDEFCNMLKK YHPVYINTHF NHPMEITKES KEACEKLANA GVPLGNQAVL
LNGINNDKFV MRCLNQELLK IRVKPYYIFQ SKHVKGTKHF NTSVDDGLEI MEYLRGYTSG
MAIPTYIVNA PKGGGKTPLL PQYLVSKGTD YVMLRTWEGK VIKMEDEPAV DIKKLIKEQA
QD
