ID   FAE_METBF               Reviewed;         178 AA.
AC   Q46AU8;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
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;
GN   Name=faeA; OrderedLocusNames=Mbar_A2060;
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, CHARACTERIZATION, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
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: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;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=30 uM for H(4)MPT {ECO:0000269|PubMed:16075199};
CC         KM=0.1 mM for formaldehyde {ECO:0000269|PubMed:16075199};
CC         Vmax=13 umol/min/mg enzyme {ECO:0000269|PubMed:16075199};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16075199}.
CC   -!- SIMILARITY: Belongs to the formaldehyde-activating enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; CP000099; AAZ70994.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q46AU8; -.
DR   SMR; Q46AU8; -.
DR   STRING; 269797.Mbar_A2060; -.
DR   EnsemblBacteria; AAZ70994; AAZ70994; Mbar_A2060.
DR   KEGG; mba:Mbar_A2060; -.
DR   eggNOG; arCOG00104; Archaea.
DR   HOGENOM; CLU_105382_0_0_2; -.
DR   OMA; ETAFCNA; -.
DR   SABIO-RK; Q46AU8; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016840; F:carbon-nitrogen lyase activity; IEA:InterPro.
DR   GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.230.60; -; 1.
DR   InterPro; IPR014826; HCHO-activating_enzyme.
DR   InterPro; IPR037075; HCHO-activating_enzyme_sf.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   Pfam; PF08714; Fae; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   TIGRFAMs; TIGR03126; one_C_fae; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Lyase.
FT   CHAIN           1..178
FT                   /note="5,6,7,8-tetrahydromethanopterin hydro-lyase"
FT                   /id="PRO_0000235169"
FT   ACT_SITE        33
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         35
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   178 AA;  19171 MW;  834AFFBDB26B9FAF CRC64;
     MFIKYAEVLN LVKNILKSMV GEALIGSGPE VAHIDLVIGP RGGSVEAAFM NSLAMPRQGH
     TPLLAVLEPN IQPKPTTLIV NKVTIKNVSQ AALMFGPAQA AVAKAVMDSV ADGVLPEEQA
     DDIFIIVSVF IEWDAKDKDK VYEFNYEATK LAIARAMEGR PTVEEALAKK DSANHPFA