{PDOC00684}
{PS00876; IDO_1}
{PS00877; IDO_2}
{BEGIN}
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* Indoleamine 2,3-dioxygenase signatures *
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Indoleamine 2,3-dioxygenase (EC 1.13.11.42) (IDO) [1] is an enzyme responsible
for the  conversion of tryptophan and other indole derivatives to kynurenines.
In mammals, IDO is induced by interferon-gamma (IFN-gamma) and responsible for
some of  its  anti-proliferative  effects.  The  degradative  action of IDO on
tryptophan leads  to cell death by starvation of this essential and relatively
scarce amino acid. IDO is a heme-containing enzyme of about 400 amino acids.

Other proteins that are evolutionarily related to IDO are:

 - Myoglobin  from  the  red  muscle  of  the  gastropods  Nordotis madaka and
   Sulculus diversicolor  [2].  These  unusual globins lack enzymatic activity
   but have kept the heme group.
 - Yeast hypothetical protein YJR078w.

As a  signature  for  the  IDO  family, we selected two conserved regions. The
first is  located    in  the central section and is rich in glycine and serine
residues; the  second  is  located  in  the  second  third of the sequence and
contains a  conserved  histidine  that could serve as a proximal ligand to the
heme iron.

-Consensus pattern: G-G-S-[AN]-[GA]-Q-S-S-x(2)-Q
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: 1.

-Consensus pattern: [FY]-L-[DQ]-[DE]-[LIVM]-x(2)-Y-M-x(3)-H-[KR]
                    [The H is a heme ligand]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: May 2004 / Text revised.

[ 1] Taylor M.W., Feng G.S.
     "Relationship between interferon-gamma, indoleamine 2,3-dioxygenase,
     and tryptophan catabolism."
     FASEB J. 5:2516-2522(1991).
     PubMed=1907934
[ 2] Suzuki T.
     "Abalone myoglobins evolved from indoleamine dioxygenase: the
     cDNA-derived amino acid sequence of myoglobin from Nordotis madaka."
     J. Protein Chem. 13:9-13(1994).
     PubMed=8011076

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