AC   MF_01527;
DC   Protein; auto
c?   <OC:Bacteria>
TR   HAMAP; MF_01527_B; -; 1; level=0
c?   <OC:Archaea>
TR   HAMAP; MF_01527_A; -; 1; level=0
XX
Names: GTP_cyclohydrol
XX
case <OC:Bacteria>
ID   GCH4
DE   RecName: Full=GTP cyclohydrolase FolE2;
DE            EC=3.5.4.16;
GN   Name=folE2;
end case
case <OC:Archaea>
ID   MPTA
DE   RecName: Full=GTP cyclohydrolase MptA;
DE            EC=3.5.4.39;
DE   AltName: Full=GTP cyclohydrolase IV;
GN   Name=mptA;
end case
XX
case <OC:Bacteria>
CC   -!- FUNCTION: Converts GTP to 7,8-dihydroneopterin triphosphate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate +
CC         H(+); Xref=Rhea:RHEA:17473, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:37565, ChEBI:CHEBI:58462; EC=3.5.4.16;
CC   -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC       biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
end case
case <OC:Archaea>
CC   -!- FUNCTION: Converts GTP to 7,8-dihydro-D-neopterin 2',3'-cyclic
CC       phosphate, the first intermediate in the biosynthesis of coenzyme
CC       methanopterin.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = 7,8-dihydroneopterin 2',3'-cyclic phosphate +
CC         diphosphate + formate + H(+); Xref=Rhea:RHEA:25860,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:58854; EC=3.5.4.39;
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC       Note=Binds 1 Fe(2+) ion per subunit.;
CC   -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin
CC       biosynthesis.
CC   -!- SUBUNIT: Homodimer.
end case
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase IV family.
XX
DR   Pfam; PF02649; GCHY-1; 1; trigger=no
DR   NCBIfam; TIGR00294; TIGR00294; 1; trigger=no
XX
KW   Hydrolase
case <OC:Archaea>
KW   Iron
KW   Metal-binding
end case
XX
case <OC:Bacteria>
GO   GO:0003934; F:GTP cyclohydrolase I activity
end case
case <OC:Archaea>
GO   GO:0003933; F:GTP cyclohydrolase activity
GO   GO:0005506; F:iron ion binding
end case
XX
FT   From: GCH4_BACSU (P94398)
case <OC:Bacteria>
FT   SITE            183
FT                   /note="May be catalytically important"
FT   Condition: C
end case
FT   From: MPTA_METJA (Q58185)
case <OC:Archaea>
FT   SITE            160
FT                   /note="May be catalytically important"
FT   Condition: C
end case
XX
Size: 251-367;
Related: None;
Template: Q58185; P94398; Q5F9K6; Q9WXP6;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in BURO1, BURO0, BURCH, BURL3, DECAR, CUPMC, METAR
Plasmid: in KLEPN
Comments: The bacterial GTP cyclohydrolases of this family share the same function as the
 GTP cyclohydrolases of the MF_00223 family (GTP cyclohydrolases 1), without having any
 sequence homology. They are orthologs to the archaeal GTP cyclohydrolases (mptA), which
 have a new catalytic activity that is different from that of the bacterial cyclohydrolases.
XX
# Revision 1.38 2023/06/01
//