Uniprot ID	E5R4J3
Uniprot Name	MAP22_LEPMJ
Taxonomy ID	985895
Sequence	M A A Q V E D D V A N L K L D D S T T K P T N G T S Q P D S K L S A E A E D S D D D A E G D G N G T G E A G A D G A A K K K K K R K P R K K K K A G T S A T A G A K S Q T S P P R V L I S D L F P N D S Y P E G E I C E Y R D E N S Y R T T N E E K R H L D R M N N D F L T D Y R K G A E I H R Q V R Q W A A N W I K P G M T L T E I A E G I E D S V R A L T G H Q G L E E G D A Q K A G M G F P T G L S I N H C A A H Y T P N A G N K V V V N Y E D V M K V D F G V H I N G R I V D S A F T K T F D P V Y D P L V E A C K A A T N A G I K E A G I D V R M S D I G A A I Q E V M E S Y E V E I G G K M L P V K C I R N L N G H S I G H Y T I H G G K T V P I V K G S D Q T K M E E G E T F A I E T F G S T G K G Y V R D D M E T S H Y A L R P D A P K V A L R I S S A K S L L A S I T K N F G T L P F C R R Y L D R L G H D K Y L L G L N N L V S S G I V E A Y P P L C D I K G S W T A Q S E H T F V L R P T C K E V L S R G D D Y
Cofactor	COFACTOR: Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000255|HAMAP-Rule:MF_03175}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03175}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_03175}; Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|HAMAP-Rule:MF_03175}; 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_03175};
Active site	No current data
Pfam	PF00557
InterPro	IPR036005 IPR000994 IPR001714 IPR002468 IPR018349 IPR036388 IPR036390