FAE_METEA
ID FAE_METEA Reviewed; 170 AA.
AC Q9FA38; C5B145;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 117.
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=fae; OrderedLocusNames=MexAM1_META1p1766;
OS Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS 9133 / AM1) (Methylobacterium extorquens).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=272630;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9651254; DOI=10.1126/science.281.5373.99;
RA Chistoserdova L.V., Vorholt J.A., Thauer R.K., Lidstrom M.E.;
RT "C1 transfer enzymes and coenzymes linking methylotrophic bacteria and
RT methanogenic Archaea.";
RL Science 281:99-102(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA Lidstrom M.E.;
RT "Methylobacterium genome sequences: a reference blueprint to investigate
RT microbial metabolism of C1 compounds from natural and industrial sources.";
RL PLoS ONE 4:E5584-E5584(2009).
RN [3]
RP PROTEIN SEQUENCE OF 2-41, FUNCTION, CATALYTIC ACTIVITY, DISRUPTION
RP PHENOTYPE, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP AND NOMENCLATURE.
RX PubMed=11073907; DOI=10.1128/jb.182.23.6645-6650.2000;
RA Vorholt J.A., Marx C.J., Lidstrom M.E., Thauer R.K.;
RT "Novel formaldehyde-activating enzyme in Methylobacterium extorquens AM1
RT required for growth on methanol.";
RL J. Bacteriol. 182:6645-6650(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEX WITH
RP METHYLENE-H(4)MPT, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ACTIVITY
RP REGULATION, AND REACTION MECHANISM.
RX PubMed=15632161; DOI=10.1074/jbc.m412320200;
RA Acharya P., Goenrich M., Hagemeier C.H., Demmer U., Vorholt J.A.,
RA Thauer R.K., Ermler U.;
RT "How an enzyme binds the C1 carrier tetrahydromethanopterin. Structure of
RT the tetrahydromethanopterin-dependent formaldehyde-activating enzyme (Fae)
RT from Methylobacterium extorquens AM1.";
RL J. Biol. Chem. 280:13712-13719(2005).
CC -!- FUNCTION: Catalyzes the condensation of formaldehyde with
CC tetrahydromethanopterin (H(4)MPT) to 5,10-
CC methylenetetrahydromethanopterin, a reaction which also proceeds
CC spontaneously, but at a lower rate than that of the enzyme-catalyzed
CC reaction. Is an essential enzyme for methylotrophic energy metabolism
CC and formaldehyde detoxification of this bacterium.
CC {ECO:0000269|PubMed:11073907, ECO:0000269|PubMed:15632161}.
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 Evidence={ECO:0000269|PubMed:11073907, ECO:0000269|PubMed:15632161};
CC -!- ACTIVITY REGULATION: Inhibited by the addition of an excess of H4F.
CC {ECO:0000269|PubMed:15632161}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 mM for formaldehyde {ECO:0000269|PubMed:11073907};
CC Note=The KM for H(4)MPT is higher than 60 uM.;
CC pH dependence:
CC Optimum pH is 7-7.5. {ECO:0000269|PubMed:11073907};
CC -!- PATHWAY: One-carbon metabolism; formaldehyde degradation; formate from
CC formaldehyde (H(4)MPT route): step 1/5.
CC -!- SUBUNIT: Homopentamer. {ECO:0000269|PubMed:11073907,
CC ECO:0000269|PubMed:15632161}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11073907}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow on
CC methanol but exhibit wild-type growth on succinate. In addition, mutant
CC is shown to be formaldehyde sensitive. {ECO:0000269|PubMed:11073907}.
CC -!- SIMILARITY: Belongs to the formaldehyde-activating enzyme family.
CC {ECO:0000305}.
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DR EMBL; AF032114; AAG32954.1; -; Genomic_DNA.
DR EMBL; CP001510; ACS39609.1; -; Genomic_DNA.
DR RefSeq; WP_003604760.1; NC_012988.1.
DR PDB; 1Y5Y; X-ray; 2.00 A; A/B/C/D/E=2-170.
DR PDB; 1Y60; X-ray; 1.90 A; A/B/C/D/E=2-170.
DR PDBsum; 1Y5Y; -.
DR PDBsum; 1Y60; -.
DR AlphaFoldDB; Q9FA38; -.
DR SMR; Q9FA38; -.
DR STRING; 272630.MexAM1_META1p1766; -.
DR DrugBank; DB03481; 5,10-Dimethylene Tetrahydromethanopterin.
DR EnsemblBacteria; ACS39609; ACS39609; MexAM1_META1p1766.
DR KEGG; mea:Mex_1p1766; -.
DR eggNOG; COG1795; Bacteria.
DR HOGENOM; CLU_105382_0_0_5; -.
DR OMA; ETAFCNA; -.
DR OrthoDB; 1129286at2; -.
DR BioCyc; MetaCyc:MON-4002; -.
DR BRENDA; 4.2.1.147; 3296.
DR SABIO-RK; Q9FA38; -.
DR UniPathway; UPA00562; UER00701.
DR EvolutionaryTrace; Q9FA38; -.
DR Proteomes; UP000009081; Chromosome.
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 GO; GO:0046294; P:formaldehyde catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
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 3D-structure; Cytoplasm; Detoxification; Direct protein sequencing; Lyase;
KW One-carbon metabolism.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11073907"
FT CHAIN 2..170
FT /note="5,6,7,8-tetrahydromethanopterin hydro-lyase"
FT /id="PRO_0000087171"
FT ACT_SITE 22
FT /note="Proton donor"
FT BINDING 24
FT /ligand="substrate"
FT BINDING 53
FT /ligand="substrate"
FT BINDING 71
FT /ligand="substrate"
FT BINDING 73
FT /ligand="substrate"
FT BINDING 88
FT /ligand="substrate"
FT STRAND 8..14
FT /evidence="ECO:0007829|PDB:1Y60"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:1Y60"
FT STRAND 21..29
FT /evidence="ECO:0007829|PDB:1Y60"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:1Y60"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1Y5Y"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:1Y60"
FT STRAND 63..72
FT /evidence="ECO:0007829|PDB:1Y60"
FT HELIX 77..83
FT /evidence="ECO:0007829|PDB:1Y60"
FT HELIX 86..100
FT /evidence="ECO:0007829|PDB:1Y60"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:1Y60"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:1Y60"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:1Y60"
FT HELIX 127..146
FT /evidence="ECO:0007829|PDB:1Y60"
FT HELIX 152..158
FT /evidence="ECO:0007829|PDB:1Y60"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:1Y60"
SQ SEQUENCE 170 AA; 18091 MW; 13BB66B298A44C32 CRC64;
MAKITKVQVG EALVGDGNEV AHIDLIIGPR GSPAETAFCN GLVNNKHGFT SLLAVIAPNL
PCKPNTLMFN KVTINDARQA VQMFGPAQHG VAMAVQDAVA EGIIPADEAD DLYVLVGVFI
HWEAADDAKI QKYNYEATKL SIQRAVNGEP KASVVTEQRK SATHPFAANA
