ID   D1Z2Q4_METPS            Unreviewed;       396 AA.
AC   D1Z2Q4;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=Bifunctional enzyme Fae/Hps {ECO:0000256|HAMAP-Rule:MF_01268};
DE   Includes:
DE     RecName: Full=5,6,7,8-tetrahydromethanopterin hydro-lyase {ECO:0000256|HAMAP-Rule:MF_01268};
DE              EC=4.2.1.147 {ECO:0000256|HAMAP-Rule:MF_01268};
DE     AltName: Full=Formaldehyde-activating enzyme {ECO:0000256|HAMAP-Rule:MF_01268};
DE              Short=Fae {ECO:0000256|HAMAP-Rule:MF_01268};
DE   Includes:
DE     RecName: Full=3-hexulose-6-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_01268};
DE              Short=HPS {ECO:0000256|HAMAP-Rule:MF_01268};
DE              EC=4.1.2.43 {ECO:0000256|HAMAP-Rule:MF_01268};
DE     AltName: Full=D-arabino-3-hexulose-6-phosphate formaldehyde lyase {ECO:0000256|HAMAP-Rule:MF_01268};
GN   Name=fae {ECO:0000313|EMBL:BAI62976.1};
GN   Synonyms=fae-hps {ECO:0000256|HAMAP-Rule:MF_01268}, hps
GN   {ECO:0000313|EMBL:BAI62976.1};
GN   OrderedLocusNames=MCP_2904 {ECO:0000313|EMBL:BAI62976.1};
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI62976.1, ECO:0000313|Proteomes:UP000001882};
RN   [1] {ECO:0000313|Proteomes:UP000001882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC   {ECO:0000313|Proteomes:UP000001882};
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(2011).
CC   -!- FUNCTION: Catalyzes the condensation of formaldehyde with
CC       tetrahydromethanopterin (H(4)MPT) to 5,10-
CC       methylenetetrahydromethanopterin. {ECO:0000256|HAMAP-Rule:MF_01268}.
CC   -!- FUNCTION: Catalyzes the reversible formation of ribulose-5-phosphate
CC       and formaldehyde from 3-hexulose-6-phosphate. {ECO:0000256|HAMAP-
CC       Rule:MF_01268}.
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01268};
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         Evidence={ECO:0000256|HAMAP-Rule:MF_01268};
CC   -!- PATHWAY: Carbohydrate biosynthesis; D-ribose 5-phosphate biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01268}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the HPS/KGPDC family.
CC       HPS subfamily. {ECO:0000256|HAMAP-Rule:MF_01268}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the formaldehyde-
CC       activating enzyme family. {ECO:0000256|HAMAP-Rule:MF_01268}.
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DR   EMBL; AP011532; BAI62976.1; -; Genomic_DNA.
DR   AlphaFoldDB; D1Z2Q4; -.
DR   STRING; 304371.MCP_2904; -.
DR   KEGG; mpd:MCP_2904; -.
DR   PATRIC; fig|304371.9.peg.2973; -.
DR   eggNOG; arCOG00103; Archaea.
DR   InParanoid; D1Z2Q4; -.
DR   OrthoDB; 64276at2157; -.
DR   UniPathway; UPA00293; -.
DR   Proteomes; UP000001882; Chromosome.
DR   GO; GO:0016840; F:carbon-nitrogen lyase activity; IEA:InterPro.
DR   GO; GO:0043801; F:hexulose-6-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016836; F:hydro-lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:InterPro.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd04726; KGPDC_HPS; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.30.230.60; Formaldehyde-activating enzyme; 1.
DR   HAMAP; MF_01268; Fae_Hps; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR020868; Fae/Hps.
DR   InterPro; IPR014826; HCHO-activating_enzyme.
DR   InterPro; IPR037075; HCHO-activating_enzyme_sf.
DR   InterPro; IPR041710; HPS/KGPDC.
DR   InterPro; IPR001754; OMPdeCOase_dom.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   NCBIfam; TIGR03126; one_C_fae; 1.
DR   PANTHER; PTHR35039; 3-KETO-L-GULONATE-6-PHOSPHATE DECARBOXYLASE SGBH-RELATED; 1.
DR   PANTHER; PTHR35039:SF3; 3-KETO-L-GULONATE-6-PHOSPHATE DECARBOXYLASE SGBH-RELATED; 1.
DR   Pfam; PF08714; Fae; 1.
DR   Pfam; PF00215; OMPdecase; 1.
DR   SMART; SM00934; OMPdecase; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW   Rule:MF_01268};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01268};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01268}.
FT   DOMAIN          174..378
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /evidence="ECO:0000259|SMART:SM00934"
FT   REGION          1..161
FT                   /note="Formaldehyde-activating enzyme"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01268"
FT   REGION          162..396
FT                   /note="3-hexulose-6-phosphate synthase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01268"
FT   ACT_SITE        17
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01268"
FT   BINDING         19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01268"
FT   BINDING         48
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01268"
FT   BINDING         66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01268"
FT   BINDING         68
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01268"
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01268"
SQ   SEQUENCE   396 AA;  42680 MW;  956B14C37D4C77E4 CRC64;
     MYLVGEALIG EGNEVAHIDL LVGDKAGPVG MAFANGMTNM SAGHTPLLAV VRPNLIPKPA
     TLIVPKVTVK NLEQAAQIFG PAQAAVAKAV ADAVEEGIIP KDQVESIVII VSVFVHPAAK
     DYTRIYKYNY GATRLALVRA MESFPPVDKV TFEKDRGTHA IMGYKIMRLW DPPYLQIAID
     APDLGVVERV LMQAPKNDHI IIEAGTPLIK RYGLEVISKI RAIKKDAFIV ADLKTLDTGN
     LEARMAADAT ADAVVCSGLA PLETIEKFCE EARKVGIYSI IDMLNVDNPA KVVEALKHKP
     DIVELHRGID TEGQKAEHAW GNIAGIKKAA GGKKLLVAVA GGVKVENVEV AMKGGADILV
     VGRAITNAKD IEGATRAFLR AMHKDEIDQY RIMTDF
//