MFTE_MYCUA
ID MFTE_MYCUA Reviewed; 250 AA.
AC A0PM51;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Mycofactocin precursor peptide peptidase {ECO:0000305|PubMed:30183269};
DE EC=3.4.14.- {ECO:0000269|PubMed:30183269};
GN Name=mftE {ECO:0000303|PubMed:30183269};
GN OrderedLocusNames=MUL_0775 {ECO:0000312|EMBL:ABL03420.1};
OS Mycobacterium ulcerans (strain Agy99).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=362242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Agy99;
RX PubMed=17210928; DOI=10.1101/gr.5942807;
RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT "Reductive evolution and niche adaptation inferred from the genome of
RT Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL Genome Res. 17:192-200(2007).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RC STRAIN=Agy99;
RX PubMed=30183269; DOI=10.1021/acs.biochem.8b00816;
RA Ayikpoe R., Salazar J., Majestic B., Latham J.A.;
RT "Mycofactocin Biosynthesis Proceeds through 3-Amino-5-[(p-
RT hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidinone (AHDP); Direct
RT Observation of MftE Specificity toward MftA.";
RL Biochemistry 57:5379-5383(2018).
CC -!- FUNCTION: Peptidase involved in the biosynthesis of the enzyme cofactor
CC mycofactocin (MFT). Catalyzes cleavage of the MftC-modified MftA
CC peptide to liberate its final two residues, which consist of a cross-
CC linked valine-decarboxylated tyrosine dipeptide (named 3-amino-5-[(4-
CC hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidin-2-one or ADHP).
CC {ECO:0000269|PubMed:30183269}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[mycofactocin precursor peptide]-C-terminal glycyl-N-{5-[(4-
CC hydroxyphenyl)methyl]-4,4-dimethyl-2-oxopyrrolidin-3-yl}acetamide +
CC H2O = 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidin-
CC 2-one + [mycofactocin precursor peptide]-C-terminal glycine;
CC Xref=Rhea:RHEA:65504, Rhea:RHEA-COMP:16818, Rhea:RHEA-COMP:16819,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:83148, ChEBI:CHEBI:150863,
CC ChEBI:CHEBI:156518; Evidence={ECO:0000269|PubMed:30183269};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:30183269};
CC Note=MftE appears to bind one Fe(2+) and one Zn(2+) ion per subunit.
CC Fe(2+) seems to be catalytically active while Zn(2+) could play an
CC auxiliary role. {ECO:0000269|PubMed:30183269};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:30183269};
CC -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:30183269}.
CC -!- SIMILARITY: Belongs to the creatininase superfamily. {ECO:0000305}.
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DR EMBL; CP000325; ABL03420.1; -; Genomic_DNA.
DR RefSeq; WP_011739045.1; NC_008611.1.
DR AlphaFoldDB; A0PM51; -.
DR SMR; A0PM51; -.
DR STRING; 362242.MUL_0775; -.
DR EnsemblBacteria; ABL03420; ABL03420; MUL_0775.
DR KEGG; mul:MUL_0775; -.
DR eggNOG; COG1402; Bacteria.
DR HOGENOM; CLU_055029_4_0_11; -.
DR OMA; PCFLWSG; -.
DR BioCyc; MetaCyc:MON-21115; -.
DR Proteomes; UP000000765; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.10310; -; 1.
DR InterPro; IPR024087; Creatininase-like_sf.
DR InterPro; IPR003785; Creatininase/forma_Hydrolase.
DR InterPro; IPR023871; MftE.
DR PANTHER; PTHR35005; PTHR35005; 1.
DR Pfam; PF02633; Creatininase; 1.
DR SUPFAM; SSF102215; SSF102215; 1.
DR TIGRFAMs; TIGR03964; mycofact_creat; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Iron; Manganese; Metal-binding; Protease; Zinc.
FT CHAIN 1..250
FT /note="Mycofactocin precursor peptide peptidase"
FT /id="PRO_0000452052"
FT BINDING 38
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P83772"
FT BINDING 40
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P83772"
FT BINDING 49
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P83772"
FT BINDING 49
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P83772"
FT BINDING 127
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P83772"
FT BINDING 166
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P83772"
SQ SEQUENCE 250 AA; 26103 MW; EF15499A22ABFD36 CRC64;
MNSSYHRRVP VLGELGTSTS SQLPSTWPSI LIPLGSTEQH GPHLPLDTDT RIATAVGRAV
ATRMHGRLTQ CQPGWLLAPP IAYGASGEHQ SFAGTISIGA EALRVLLLEY GRSAACWADR
LVFVNGHGGN VEALRGAVRQ LRAEGRDAGW SACGSAGGDA HAGHTETSVL LHISPEVVLT
DRLSAGNAAP LAELLPSLRR GGVAAVSPIG VLGDPTTATA VEGRRIFAEM VDDCVSRIAR
WTPGPDGMLT
