Uniprot ID	B6YTG0
Uniprot Name	MAP2_THEON
Taxonomy ID	523850
Sequence	M D E R E A L I K A G E I A R Q V K K E V I S L I K P G T K L Y D I A E F V E R R I I E L G G K P A F P C N L S I N E I A A H Y T P Y K G D E T V L K E G D Y L K V D I G V H V D G Y I A D T A L T F R V G M E E D D L V T A A R E A L E N A I K V I R A G I K I N E I G K A I E E T I R G Y G F N P I V N L S G H K I E R Y K L H A G I S I P N I Y R P A D S Y V L K E G D V I A I E P F A T T G A G Q V I E V P P A L I F M Y L R D R P V R M A Q A R R V L M H I K R E Y N G L P F A Y R W L Q G F M P E G Q L K L A L A Q L D R V G A I Y S Y P I L R E V R G G L V A Q F E H T V I V E K E G A Y I T T
Cofactor	COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250, ECO:0000269|PubMed:16761197}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250, ECO:0000269|PubMed:16761197}; Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000250, ECO:0000269|PubMed:16761197}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250, ECO:0000269|PubMed:16761197}; 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. 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. The enzyme is active with cobalt, nickel, manganese and divalent iron ions. {ECO:0000250, ECO:0000269|PubMed:16761197};
Active site	No current data
Pfam	PF00557
InterPro	IPR036005 IPR028595 IPR000994 IPR001714 IPR002468 IPR018349 IPR036388 IPR036390