ID   FAEHP_METBF             Reviewed;         392 AA.
AC   Q46DY5;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Bifunctional enzyme Fae/Hps {ECO:0000255|HAMAP-Rule:MF_01268};
DE   Includes:
DE     RecName: Full=5,6,7,8-tetrahydromethanopterin hydro-lyase {ECO:0000255|HAMAP-Rule:MF_01268};
DE              EC=4.2.1.147 {ECO:0000255|HAMAP-Rule:MF_01268, ECO:0000269|PubMed:16075199};
DE     AltName: Full=Formaldehyde-activating enzyme {ECO:0000255|HAMAP-Rule:MF_01268, ECO:0000303|PubMed:16075199};
DE              Short=Fae {ECO:0000255|HAMAP-Rule:MF_01268, ECO:0000303|PubMed:16075199};
DE   Includes:
DE     RecName: Full=3-hexulose-6-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_01268, ECO:0000303|PubMed:16075199};
DE              Short=HPS {ECO:0000255|HAMAP-Rule:MF_01268, ECO:0000303|PubMed:16075199};
DE              EC=4.1.2.43 {ECO:0000255|HAMAP-Rule:MF_01268, ECO:0000269|PubMed:16075199};
DE     AltName: Full=D-arabino-3-hexulose-6-phosphate formaldehyde lyase {ECO:0000255|HAMAP-Rule:MF_01268};
GN   Name=faeB-hpsB {ECO:0000303|PubMed:16075199};
GN   OrderedLocusNames=Mbar_A0935;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16075199; DOI=10.1007/s00203-005-0008-1;
RA   Goenrich M., Thauer R.K., Yurimoto H., Kato N.;
RT   "Formaldehyde activating enzyme (Fae) and hexulose-6-phosphate synthase
RT   (Hps) in Methanosarcina barkeri: a possible function in ribose-5-phosphate
RT   biosynthesis.";
RL   Arch. Microbiol. 184:41-48(2005).
CC   -!- FUNCTION: Catalyzes the condensation of formaldehyde with
CC       tetrahydromethanopterin (H(4)MPT) to 5,10-
CC       methylenetetrahydromethanopterin. {ECO:0000255|HAMAP-Rule:MF_01268,
CC       ECO:0000269|PubMed:16075199}.
CC   -!- FUNCTION: Catalyzes the reversible formation of ribulose-5-phosphate
CC       and formaldehyde from 3-hexulose-6-phosphate. {ECO:0000255|HAMAP-
CC       Rule:MF_01268, ECO:0000269|PubMed:16075199}.
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:0000255|HAMAP-
CC         Rule:MF_01268, ECO:0000269|PubMed:16075199};
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:0000255|HAMAP-Rule:MF_01268,
CC         ECO:0000269|PubMed:16075199};
CC   -!- PATHWAY: Carbohydrate biosynthesis; D-ribose 5-phosphate biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01268, ECO:0000303|PubMed:16075199}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the formaldehyde-
CC       activating enzyme family. {ECO:0000255|HAMAP-Rule:MF_01268}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the HPS/KGPDC family.
CC       HPS subfamily. {ECO:0000255|HAMAP-Rule:MF_01268}.
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DR   EMBL; CP000099; AAZ69907.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q46DY5; -.
DR   SMR; Q46DY5; -.
DR   STRING; 269797.Mbar_A0935; -.
DR   PaxDb; 269797-Mbar_A0935; -.
DR   KEGG; mba:Mbar_A0935; -.
DR   eggNOG; arCOG00103; Archaea.
DR   HOGENOM; CLU_701335_0_0_2; -.
DR   OrthoDB; 64276at2157; -.
DR   UniPathway; UPA00293; -.
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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Lyase; Multifunctional enzyme.
FT   CHAIN           1..392
FT                   /note="Bifunctional enzyme Fae/Hps"
FT                   /id="PRO_0000235168"
FT   REGION          1..161
FT                   /note="Formaldehyde-activating enzyme"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT   REGION          162..392
FT                   /note="3-hexulose-6-phosphate synthase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT   ACT_SITE        17
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT   BINDING         19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT   BINDING         48
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT   BINDING         66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT   BINDING         68
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
SQ   SEQUENCE   392 AA;  42415 MW;  AE132C4FBBAC00A1 CRC64;
     MFQIGEALMG QGAELAHVDL MIGDKGGPVG QAFANGLTQL SVGHTPLLSV IRPNLPPKPS
     TLIIPKVTVK NMEQAGKIFG PAQAAVAKAV ADSVEEGVIS KDQVEEIVIV ASVFIHPDAQ
     DYNKIYRYNY GATKLAIKRA LGGFPDINTV LEESNKSTHA IMGFKVTRLW DPPYLQVAFD
     NPDIEFVQSA ISQIPKSDHV IIEAGTPLIK RYGMDVISRI REVRPDAFIV ADLKTLDTGN
     LEARMVADAA GDAIVVSALA PISTIDKLIE EAHKTGIYAV MDTLNQQDPI SVLKQLKVMP
     DVIELHRGID IEATEHAWGN IAEIKKIAPK ILVAVAGGVR LDKVPVALGQ GADILVVGRA
     ITNSKDVREV AEQFINSLNK PEIDQFRVMT DF
//