UniProt functional annotation for P9WK19



	UniProt functional annotation for P9WK19

UniProt code: P9WK19.

Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).

Taxonomy: Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.

Function: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. {ECO:0000255|HAMAP- Rule:MF_01974, ECO:0000269|PubMed:19688379, ECO:0000269|PubMed:20038112}.

Catalytic activity: Reaction=Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.; EC=3.4.11.18; Evidence={ECO:0000255|HAMAP-Rule:MF_01974};

Cofactor: Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:15882055, ECO:0000269|PubMed:20038112}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_01974}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:20038112, ECO:0000269|PubMed:21465667}; Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:20038112}; Note=Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site. {ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000305|PubMed:20038112};

Activity regulation: Inhibited by bengamide derivatives and by various metalloform-selective inhibitors. {ECO:0000269|PubMed:20038112, ECO:0000269|PubMed:21465667}.

Biophysicochemical properties: Kinetic parameters: KM=58 uM for Met-Gly-Met-Met (at pH 7.5 and at 37 degrees Celsius) {ECO:0000269|PubMed:19688379, ECO:0000269|PubMed:20038112}; KM=394 uM for Met-Ala-Ser (at pH 7.5 and at 37 degrees Celsius) {ECO:0000269|PubMed:19688379, ECO:0000269|PubMed:20038112}; Temperature dependence: Optimum temperature is 37 degrees Celsius. It lost all its activities at 55 degrees Celsius. {ECO:0000269|PubMed:19688379, ECO:0000269|PubMed:20038112};

Subunit: Monomer. {ECO:0000255|HAMAP-Rule:MF_01974}.

Mass spectrometry: Mass=32516; Method=MALDI; Evidence={ECO:0000269|PubMed:19688379};

Similarity: Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01974}.

Annotations taken from UniProtKB at the EBI.


Organism:		Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Taxonomy:		Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.



Function:		Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. {ECO:0000255\|HAMAP- Rule:MF_01974, ECO:0000269\|PubMed:19688379, ECO:0000269\|PubMed:20038112}.


Catalytic activity:		Reaction=Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.; EC=3.4.11.18; Evidence={ECO:0000255\|HAMAP-Rule:MF_01974};
Cofactor:		Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000255\|HAMAP-Rule:MF_01974, ECO:0000269\|PubMed:15882055, ECO:0000269\|PubMed:20038112}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255\|HAMAP-Rule:MF_01974}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255\|HAMAP-Rule:MF_01974, ECO:0000269\|PubMed:20038112, ECO:0000269\|PubMed:21465667}; Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255\|HAMAP-Rule:MF_01974, ECO:0000269\|PubMed:20038112}; Note=Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site. {ECO:0000255\|HAMAP-Rule:MF_01974, ECO:0000305\|PubMed:20038112};
Activity regulation:		Inhibited by bengamide derivatives and by various metalloform-selective inhibitors. {ECO:0000269\|PubMed:20038112, ECO:0000269\|PubMed:21465667}.
Biophysicochemical properties:		Kinetic parameters: KM=58 uM for Met-Gly-Met-Met (at pH 7.5 and at 37 degrees Celsius) {ECO:0000269\|PubMed:19688379, ECO:0000269\|PubMed:20038112}; KM=394 uM for Met-Ala-Ser (at pH 7.5 and at 37 degrees Celsius) {ECO:0000269\|PubMed:19688379, ECO:0000269\|PubMed:20038112}; Temperature dependence: Optimum temperature is 37 degrees Celsius. It lost all its activities at 55 degrees Celsius. {ECO:0000269\|PubMed:19688379, ECO:0000269\|PubMed:20038112};
Subunit:		Monomer. {ECO:0000255\|HAMAP-Rule:MF_01974}.
Mass spectrometry:		Mass=32516; Method=MALDI; Evidence={ECO:0000269\|PubMed:19688379};
Similarity:		Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. {ECO:0000255\|HAMAP-Rule:MF_01974}.