AC   MF_01268;
DC   Protein; auto
TR   HAMAP; MF_01268; -; 1; level=0
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Names: Fae_Hps
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ID   FAEHP
DE   RecName: Full=Bifunctional enzyme Fae/Hps;
DE   Includes:
DE     RecName: Full=5,6,7,8-tetrahydromethanopterin hydro-lyase;
DE              EC=4.2.1.147;
DE     AltName: Full=Formaldehyde-activating enzyme;
DE              Short=Fae;
DE   Includes:
DE     RecName: Full=3-hexulose-6-phosphate synthase;
DE              Short=HPS;
DE              EC=4.1.2.43;
DE     AltName: Full=D-arabino-3-hexulose-6-phosphate formaldehyde lyase;
GN   Name=fae-hps;
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CC   -!- FUNCTION: Catalyzes the condensation of formaldehyde with
CC       tetrahydromethanopterin (H(4)MPT) to 5,10-
CC       methylenetetrahydromethanopterin.
CC   -!- FUNCTION: Catalyzes the reversible formation of ribulose-5-phosphate
CC       and formaldehyde from 3-hexulose-6-phosphate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6,7,8-tetrahydromethanopterin + formaldehyde = 5,10-
CC         methylenetetrahydromethanopterin + H2O; Xref=Rhea:RHEA:24678,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16842, ChEBI:CHEBI:57818,
CC         ChEBI:CHEBI:58103; EC=4.2.1.147;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-ribulose 5-phosphate + formaldehyde = D-arabino-hex-3-ulose
CC         6-phosphate; Xref=Rhea:RHEA:25201, ChEBI:CHEBI:16842,
CC         ChEBI:CHEBI:58121, ChEBI:CHEBI:58542; EC=4.1.2.43;
CC   -!- PATHWAY: Carbohydrate biosynthesis; D-ribose 5-phosphate biosynthesis.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the formaldehyde-
CC       activating enzyme family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the HPS/KGPDC family.
CC       HPS subfamily.
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DR   Pfam; PF00215; OMPdecase; 1; trigger=no
DR   NCBIfam; TIGR03126; one_C_fae; 1; trigger=no
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KW   Carbohydrate metabolism
KW   Lyase
KW   Multifunctional enzyme
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GO   GO:0043801; F:hexulose-6-phosphate synthase activity
GO   GO:0016836; F:hydro-lyase activity
GO   GO:0016051; P:carbohydrate biosynthetic process
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FT   From: FAEHP_METBF (Q46DY5)
FT   REGION          Nter..161
FT                   /note="Formaldehyde-activating enzyme"
FT   REGION          162..Cter
FT                   /note="3-hexulose-6-phosphate synthase"
FT   ACT_SITE        17
FT                   /note="Proton donor"
FT   Condition: H
FT   BINDING         19
FT                   /ligand="substrate"
FT   Condition: D
FT   BINDING         48
FT                   /ligand="substrate"
FT   Condition: L
FT   BINDING         66
FT                   /ligand="substrate"
FT   Condition: K
FT   BINDING         68
FT                   /ligand="substrate"
FT   Condition: T
FT   BINDING         83
FT                   /ligand="substrate"
FT   Condition: Q
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Size: 375-420;
Related: None;
Template: Q46DY5; Q58842;
Scope:
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: In METJA, lacks the active site His and substrate binding sites expected to be involved in fae activity.
 Monofunctional fae enzyme exists in methylotrophic bacteria, where it is involved in energy metabolism and
 formaldehyde detoxification.
 Monofunctional HPS enzyme exists in bacteria, but functions in the opposite direction (condensation of
 ribulose 5-phosphate with formaldehyde), and is involved in C1 assimilation and/or formaldehyde detoxification.
 METBF possesses the bifunctional fae/hps enzyme, and also the two monofunctional enzymes fae and hps.
 FT lines are propagated from Methylobacterium extorquens fae enzyme, whose X-ray structure is known.
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# Revision 1.18 2023/06/01
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