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COFH1_METMA
ID   COFH1_METMA             Reviewed;         376 AA.
AC   Q8PU54;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase 1 {ECO:0000255|HAMAP-Rule:MF_01612};
DE            EC=2.5.1.147 {ECO:0000255|HAMAP-Rule:MF_01612};
DE   AltName: Full=FO synthase subunit 2 1 {ECO:0000255|HAMAP-Rule:MF_01612};
GN   Name=cofH1 {ECO:0000255|HAMAP-Rule:MF_01612}; OrderedLocusNames=MM_2495;
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 radical-mediated synthesis of 5-amino-5-(4-
CC       hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-
CC       ribitylamino)uracil and L-tyrosine. {ECO:0000255|HAMAP-Rule:MF_01612}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-
CC         methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-
CC         hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-
CC         methionine; Xref=Rhea:RHEA:55200, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15934, ChEBI:CHEBI:17319, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:58315, ChEBI:CHEBI:59789, ChEBI:CHEBI:77846,
CC         ChEBI:CHEBI:85936; EC=2.5.1.147; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01612};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01612};
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000255|HAMAP-Rule:MF_01612};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme F0 biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01612}.
CC   -!- SUBUNIT: Consists of two subunits, CofG and CofH. {ECO:0000255|HAMAP-
CC       Rule:MF_01612}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. CofH family.
CC       {ECO:0000255|HAMAP-Rule:MF_01612}.
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DR   EMBL; AE008384; AAM32191.1; -; Genomic_DNA.
DR   RefSeq; WP_011034413.1; NC_003901.1.
DR   AlphaFoldDB; Q8PU54; -.
DR   SMR; Q8PU54; -.
DR   STRING; 192952.MM_2495; -.
DR   EnsemblBacteria; AAM32191; AAM32191; MM_2495.
DR   GeneID; 44087887; -.
DR   GeneID; 66135456; -.
DR   KEGG; mma:MM_2495; -.
DR   PATRIC; fig|192952.21.peg.2856; -.
DR   eggNOG; arCOG00656; Archaea.
DR   HOGENOM; CLU_040406_1_0_2; -.
DR   OMA; ATMMFGS; -.
DR   UniPathway; UPA00072; -.
DR   Proteomes; UP000000595; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0044689; F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01612; FO_synth_sub2; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR045567; CofH/MnqC-like_C.
DR   InterPro; IPR019940; CofH_family.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR034405; F420.
DR   InterPro; IPR020050; FO_synthase_su2.
DR   InterPro; IPR007197; rSAM.
DR   PANTHER; PTHR43076; PTHR43076; 1.
DR   Pfam; PF19288; CofH_C; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDF00293; ((2_3_4_5-tetrahydroxypentyl)a; 1.
DR   SFLD; SFLDF00343; aminofutalosine_synthase_(mqnE; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR03551; F420_cofH; 1.
DR   TIGRFAMs; TIGR00423; TIGR00423; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..376
FT                   /note="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-
FT                   hydroxyphenyl transferase 1"
FT                   /id="PRO_0000141720"
FT   DOMAIN          50..275
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         64
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01612"
FT   BINDING         68
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01612"
FT   BINDING         71
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01612"
SQ   SEQUENCE   376 AA;  41949 MW;  4D33D1C3EB352D79 CRC64;
     MNSRIPEDLI ERAHRGKTTK EDALLLLEVP PFELFRFADE LRDLAAGDTV TYVVNRNINF
     TSRCTGSCGF CAFRTDDGKV LSIEEIMEKV REAEKANATE VCIQGGLLPD VGLDFYQGIV
     EAIKAEFPEM HVHSFSPMEV YHASRISEIP VKESLRRLKR SGLDTMPGTA AEILSDRVRK
     IICPAKLNTA EWIEVVTQAH AAGIPTTATM MYGHVETPEE RINHMLTIRE IQKETGGITE
     FVPLPFMPYN NPVGEKMIKE GRYATPGLED LKVYAVSRIL FHGHVDNIQA SWVKLGKKFA
     QFSLHCGVND LGGTLMEESI SRSAGACHGE MITVDELEWM IHGAGRIPKE RTTLYREAHE
     LASRNSRKIA GCGAFE
 
 
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