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Database: UniProt
Entry: A0A0E3P004_9EURY
LinkDB: A0A0E3P004_9EURY
Original site: A0A0E3P004_9EURY 
ID   A0A0E3P004_9EURY        Unreviewed;       332 AA.
AC   A0A0E3P004;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase {ECO:0000256|HAMAP-Rule:MF_01921};
DE            EC=4.1.3.44 {ECO:0000256|HAMAP-Rule:MF_01921};
DE   AltName: Full=tRNA wyosine derivatives biosynthesis protein Taw1 {ECO:0000256|HAMAP-Rule:MF_01921};
GN   Name=taw1 {ECO:0000256|HAMAP-Rule:MF_01921};
GN   ORFNames=MSMTP_3213 {ECO:0000313|EMBL:AKB26682.1};
OS   Methanosarcina sp. MTP4.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=1434100 {ECO:0000313|EMBL:AKB26682.1, ECO:0000313|Proteomes:UP000033049};
RN   [1] {ECO:0000313|EMBL:AKB26682.1, ECO:0000313|Proteomes:UP000033049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MTP4 {ECO:0000313|EMBL:AKB26682.1,
RC   ECO:0000313|Proteomes:UP000033049};
RA   Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA   Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT   "Methanogenic archaea and the global carbon cycle.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the wyosine derivatives biosynthesis pathway
CC       that catalyzes the condensation of N-methylguanine with 2 carbon atoms
CC       from pyruvate to form the tricyclic 4-demethylwyosine (imG-14) on
CC       guanosine-37 of tRNA(Phe). {ECO:0000256|HAMAP-Rule:MF_01921}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(1)-methylguanosine(37) in tRNA(Phe) + pyruvate + S-adenosyl-
CC         L-methionine = 4-demethylwyosine(37) in tRNA(Phe) + 5'-deoxyadenosine
CC         + CO2 + H2O + L-methionine; Xref=Rhea:RHEA:36347, Rhea:RHEA-
CC         COMP:10164, Rhea:RHEA-COMP:10165, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16526, ChEBI:CHEBI:17319,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:64315,
CC         ChEBI:CHEBI:73542; EC=4.1.3.44;
CC         Evidence={ECO:0000256|ARBA:ARBA00000664, ECO:0000256|HAMAP-
CC         Rule:MF_01921};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01921};
CC       Note=Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated
CC       with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000256|HAMAP-Rule:MF_01921};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01921}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01921}.
CC   -!- SIMILARITY: Belongs to the TYW1 family. {ECO:0000256|HAMAP-
CC       Rule:MF_01921}.
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DR   EMBL; CP009505; AKB26682.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E3P004; -.
DR   STRING; 1434100.MSMTP_3213; -.
DR   KEGG; metm:MSMTP_3213; -.
DR   PATRIC; fig|1434100.4.peg.4273; -.
DR   HOGENOM; CLU_007952_3_0_2; -.
DR   Proteomes; UP000033049; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0102521; F:tRNA-4-demethylwyosine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
DR   CDD; cd01335; Radical_SAM; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_01921; TYW1_archaea; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR013917; tRNA_wybutosine-synth.
DR   InterPro; IPR034556; tRNA_wybutosine-synthase.
DR   InterPro; IPR023993; TYW1_archaea.
DR   NCBIfam; TIGR03972; rSAM_TYW1; 1.
DR   PANTHER; PTHR13930; S-ADENOSYL-L-METHIONINE-DEPENDENT TRNA 4-DEMETHYLWYOSINE SYNTHASE; 1.
DR   PANTHER; PTHR13930:SF0; S-ADENOSYL-L-METHIONINE-DEPENDENT TRNA 4-DEMETHYLWYOSINE SYNTHASE TYW1-RELATED; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   Pfam; PF08608; Wyosine_form; 1.
DR   SFLD; SFLDF00284; tRNA_wybutosine-synthesizing; 1.
DR   SFLD; SFLDG01071; tRNA_wybutosine-synthesizing; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01921};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01921};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01921};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW   Rule:MF_01921};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01921};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01921}; Reference proteome {ECO:0000313|Proteomes:UP000033049};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_01921}; tRNA processing {ECO:0000256|HAMAP-Rule:MF_01921}.
FT   DOMAIN          62..299
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   BINDING         43
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01921"
FT   BINDING         56
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01921"
FT   BINDING         69
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01921"
FT   BINDING         78
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01921"
FT   BINDING         82
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01921"
FT   BINDING         85
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01921"
SQ   SEQUENCE   332 AA;  37255 MW;  570C9425C10F9663 CRC64;
     MENQNQDQSS GKPPLPFDIP DFETLLKKQG YALAGSHSAV KTCLWLKKAM NDEGFCYKGK
     FYGVASHRCL QMTPTLLCNQ SCLFCWRPTE VPVPAPGEWD SPEKIVEESI ACQRKLITGF
     GGSPNALKER WLEGNDPNNV AISLSGEPTM YPYLPELIEE YEKRGFTTFL VTNGTIPGMF
     AKVNPCQLYM SLDAPDQATY LKVCQPKSPA LWDKISESLA LMKEKSSRTV IRITLVKGVN
     MFNPEGYAEL IKKASPDFVE IKAYMHLGFS RLRLERSAMP AHAEVLEFSE QVAKHLGYEI
     ADESEISRVV LLSKDGKKSP VRKKTLEENK ET
//
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