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MFNB_METS3
ID   MFNB_METS3              Reviewed;         237 AA.
AC   A5UNQ5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=(5-formylfuran-3-yl)methyl phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00681};
DE            EC=4.2.3.153 {ECO:0000255|HAMAP-Rule:MF_00681};
DE   AltName: Full=4-(hydroxymethyl)-2-furancarboxaldehyde-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00681};
DE            Short=4-HFC-P synthase {ECO:0000255|HAMAP-Rule:MF_00681};
GN   Name=mfnB {ECO:0000255|HAMAP-Rule:MF_00681}; OrderedLocusNames=Msm_1628;
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA   Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT   human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
CC   -!- FUNCTION: Catalyzes the formation of 4-(hydroxymethyl)-2-
CC       furancarboxaldehyde phosphate (4-HFC-P) from two molecules of
CC       glyceraldehyde-3-P (GA-3-P). {ECO:0000255|HAMAP-Rule:MF_00681}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 D-glyceraldehyde 3-phosphate = 4-(hydroxymethyl)-2-
CC         furancarboxaldehyde phosphate + 2 H2O + phosphate;
CC         Xref=Rhea:RHEA:43536, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:59776, ChEBI:CHEBI:83407; EC=4.2.3.153;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00681};
CC   -!- PATHWAY: Cofactor biosynthesis; methanofuran biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00681}.
CC   -!- SIMILARITY: Belongs to the MfnB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00681}.
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DR   EMBL; CP000678; ABQ87833.1; -; Genomic_DNA.
DR   RefSeq; WP_011954643.1; NC_009515.1.
DR   AlphaFoldDB; A5UNQ5; -.
DR   SMR; A5UNQ5; -.
DR   STRING; 420247.Msm_1628; -.
DR   EnsemblBacteria; ABQ87833; ABQ87833; Msm_1628.
DR   GeneID; 5216862; -.
DR   KEGG; msi:Msm_1628; -.
DR   PATRIC; fig|420247.28.peg.1618; -.
DR   eggNOG; arCOG04482; Archaea.
DR   HOGENOM; CLU_068659_0_0_2; -.
DR   OMA; NFPWVIR; -.
DR   BioCyc; MSMI420247:GHWZ-1669-MON; -.
DR   UniPathway; UPA00080; -.
DR   Proteomes; UP000001992; Chromosome.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:2001120; P:methanofuran biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00681; MfnB; 1.
DR   InterPro; IPR007565; 4HFCP_synth.
DR   InterPro; IPR035081; 4HFCP_synth_arc.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   Pfam; PF04476; 4HFCP_synth; 1.
DR   PIRSF; PIRSF015957; UCP015957; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
PE   3: Inferred from homology;
KW   Lyase; Schiff base.
FT   CHAIN           1..237
FT                   /note="(5-formylfuran-3-yl)methyl phosphate synthase"
FT                   /id="PRO_1000044923"
FT   ACT_SITE        27
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00681"
FT   ACT_SITE        85
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00681"
SQ   SEQUENCE   237 AA;  25250 MW;  83C83942BD89D9DB CRC64;
     MLLLISPINH EEALESIKGG ADIVDVKNPK EGSLGANFPW VIRDIREITP EDKLVSATLG
     DVPYKPGTVS LAAMGAHVSG ADYIKVGLYG TKDYDEAVEV MENVAKTIKD VDNDTIVVAS
     GYADAHRVGA VDPMEIPKVA KDAGCDLAML DTAVKDGHTL FDYLSIEDLE KFVNEAHSYG
     LKTALAGSVK KEQLKPLNDI GCDVVGIRGA ACVGGDRNTG KIHHTAVAEL KELCDSF
 
 
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