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COFH2_METAC
ID   COFH2_METAC             Reviewed;         384 AA.
AC   Q8TQQ1;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01612};
GN   Name=cofH2 {ECO:0000255|HAMAP-Rule:MF_01612}; OrderedLocusNames=MA_1489;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM04903.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE010299; AAM04903.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011021503.1; NC_003552.1.
DR   AlphaFoldDB; Q8TQQ1; -.
DR   SMR; Q8TQQ1; -.
DR   STRING; 188937.MA_1489; -.
DR   EnsemblBacteria; AAM04903; AAM04903; MA_1489.
DR   GeneID; 1473377; -.
DR   KEGG; mac:MA_1489; -.
DR   HOGENOM; CLU_040406_1_0_2; -.
DR   InParanoid; Q8TQQ1; -.
DR   OMA; HVTNICK; -.
DR   OrthoDB; 26917at2157; -.
DR   PhylomeDB; Q8TQQ1; -.
DR   UniPathway; UPA00072; -.
DR   Proteomes; UP000002487; 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; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; IPR012314; Pept_M12B_GON-ADAMTSs.
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   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR03551; F420_cofH; 1.
DR   TIGRFAMs; TIGR00423; TIGR00423; 1.
DR   PROSITE; PS51046; GON; 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..384
FT                   /note="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-
FT                   hydroxyphenyl transferase 2"
FT                   /id="PRO_0000141716"
FT   DOMAIN          53..286
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         67
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"
FT   BINDING         74
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   384 AA;  42249 MW;  76CACE1179C1FA13 CRC64;
     MYMKKPAIPD DVIERVQQGK CTKEDALLLL EGNPFELFEL ANKLRASTVG DVVSYVVNRN
     IYITNKCVGT CGFCAYRTDE GYILSIEEIL KQTEEAREAG AVEVCVQGGY TPEADMEFYL
     EIIEAIKSGF PDICIHALSP MEVNYAAGLS GMSVEDALRK LKKCGLDSLT GTSAEILSDR
     VRKIICPGKI TTQQWVDTVT AAHRAGISTN STIMYGHVET LEERLDHVFT IREIQKETGG
     ISELIPMSFL PYNNPIGEKM MASGKFTSTG LEDLQLIAIS RIILHTHVNN IQATWVKLGK
     KLAQFALQCG ANDLGGTLME DQISTASGGS YGEYVSPAEF EWMIKGAGRV PIQRDTLYRK
     VEPRLPASEG LLPGYVKPKM GSKE
 
 
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