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FTR_METBU
ID   FTR_METBU               Reviewed;         297 AA.
AC   Q12VA6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Formylmethanofuran--tetrahydromethanopterin formyltransferase {ECO:0000255|HAMAP-Rule:MF_00579};
DE            Short=Ftr {ECO:0000255|HAMAP-Rule:MF_00579};
DE            EC=2.3.1.101 {ECO:0000255|HAMAP-Rule:MF_00579};
DE   AltName: Full=H4MPT formyltransferase {ECO:0000255|HAMAP-Rule:MF_00579};
GN   Name=ftr {ECO:0000255|HAMAP-Rule:MF_00579}; OrderedLocusNames=Mbur_1728;
OS   Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS   ACE-M).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX   NCBI_TaxID=259564;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX   PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA   Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA   De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA   Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA   Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA   Cavicchioli R.;
RT   "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT   burtonii: the role of genome evolution in cold adaptation.";
RL   ISME J. 3:1012-1035(2009).
CC   -!- FUNCTION: Catalyzes the reversible transfer of a formyl group from
CC       formylmethanofuran (formyl-MFR) to tetrahydromethanopterin (H(4)MPT) to
CC       produce 5-formyl tetrahydromethanopterin (5-formyl-H(4)MPT) and
CC       methanofuran (MFR). {ECO:0000255|HAMAP-Rule:MF_00579}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6,7,8-tetrahydromethanopterin + H(+) + N-formylmethanofuran
CC         = methanofuran + N(5)-formyl-5,6,7,8-tetrahydromethanopterin;
CC         Xref=Rhea:RHEA:18061, ChEBI:CHEBI:15378, ChEBI:CHEBI:57727,
CC         ChEBI:CHEBI:58018, ChEBI:CHEBI:58103, ChEBI:CHEBI:58151;
CC         EC=2.3.1.101; Evidence={ECO:0000255|HAMAP-Rule:MF_00579};
CC   -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); 5,10-
CC       methenyl-5,6,7,8-tetrahydromethanopterin from CO(2): step 2/3.
CC       {ECO:0000255|HAMAP-Rule:MF_00579}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00579}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00579}.
CC   -!- SIMILARITY: Belongs to the FTR family. {ECO:0000255|HAMAP-
CC       Rule:MF_00579}.
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DR   EMBL; CP000300; ABE52620.1; -; Genomic_DNA.
DR   RefSeq; WP_011499763.1; NC_007955.1.
DR   AlphaFoldDB; Q12VA6; -.
DR   SMR; Q12VA6; -.
DR   STRING; 259564.Mbur_1728; -.
DR   EnsemblBacteria; ABE52620; ABE52620; Mbur_1728.
DR   GeneID; 3997403; -.
DR   KEGG; mbu:Mbur_1728; -.
DR   HOGENOM; CLU_081314_0_0_2; -.
DR   OMA; VIMCPAE; -.
DR   OrthoDB; 62652at2157; -.
DR   UniPathway; UPA00640; UER00693.
DR   Proteomes; UP000001979; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030270; F:formylmethanofuran-tetrahydromethanopterin N-formyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.70.520; -; 2.
DR   HAMAP; MF_00579; FTR; 1.
DR   InterPro; IPR014053; ForMFR_H4MPT_ForTrfase.
DR   InterPro; IPR002770; ForMFR_H4MPT_ForTrfase_C.
DR   InterPro; IPR023447; ForMFR_H4MPT_ForTrfase_fd-like.
DR   InterPro; IPR022667; ForMFR_H4MPT_ForTrfase_N.
DR   Pfam; PF01913; FTR; 1.
DR   Pfam; PF02741; FTR_C; 1.
DR   PIRSF; PIRSF006414; Ftr_formyl_trnsf; 1.
DR   SUPFAM; SSF55112; SSF55112; 2.
DR   TIGRFAMs; TIGR03119; one_C_fhcD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Methanogenesis; One-carbon metabolism;
KW   Reference proteome; Transferase.
FT   CHAIN           1..297
FT                   /note="Formylmethanofuran--tetrahydromethanopterin
FT                   formyltransferase"
FT                   /id="PRO_1000025194"
SQ   SEQUENCE   297 AA;  31444 MW;  45C543D26F4F2824 CRC64;
     MELNGVEIED TFAEAFPIKI SRILITAATK RWATVAAQEA TGFGTSVIGC PAEAGIEKYA
     DASETPDGRP GVYIQFCTFG FKSLEEQLLE RVGQCILTAP TTAVFNGLPD AEKQFDTGRK
     LKYFADGTES ETEVGGRKMH VIPMMEGDFL VEDTLGAVTA IAGGNFFIFG DTQMTTLTAA
     ENAVDAIGAV DGTITPFPGG IVASGSKAGA NKYKFLKATA NEKFCPSIKD KVEGSEIPAD
     VNCVYEIVIN GLDFESIAKA TEMGIRAAVA VPGIKKITAG NYGGSLGPHK FNLHDLF
 
 
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