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MFNB_METMA
ID   MFNB_METMA              Reviewed;         234 AA.
AC   Q8PXV2;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 110.
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=MM_1114;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM30810.1; -; Genomic_DNA.
DR   RefSeq; WP_011033063.1; NC_003901.1.
DR   AlphaFoldDB; Q8PXV2; -.
DR   SMR; Q8PXV2; -.
DR   STRING; 192952.MM_1114; -.
DR   EnsemblBacteria; AAM30810; AAM30810; MM_1114.
DR   GeneID; 44085634; -.
DR   GeneID; 66137458; -.
DR   KEGG; mma:MM_1114; -.
DR   PATRIC; fig|192952.21.peg.1303; -.
DR   eggNOG; arCOG04482; Archaea.
DR   HOGENOM; CLU_068659_0_0_2; -.
DR   OMA; NFPWVIR; -.
DR   UniPathway; UPA00080; -.
DR   Proteomes; UP000000595; 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; Reference proteome; Schiff base.
FT   CHAIN           1..234
FT                   /note="(5-formylfuran-3-yl)methyl phosphate synthase"
FT                   /id="PRO_0000134867"
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   234 AA;  24942 MW;  4596C559DAD570BA CRC64;
     MKLLVSPINS EEAIIASIGG ADIVDVKNPK EGSLGANFPW VIREVKAVVN GRQPISATIG
     DFNYKPGTAA LAALGAAVAG ADYIKVGLYD IQTESQALEL LTKITRAVKD YNPLKKVVAS
     GYSDYKRINS ISPLLLPAVA AEAGVDVVMV DTGVKDGKST FEFMDEKELK EFTDLAHSYG
     LENAIAGSLK FEDIPLLERI GPDIIGVRGM VCGGDRSTSI RQELVEKLVA ECQA
 
 
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