COFH_HALSA
ID COFH_HALSA Reviewed; 453 AA.
AC Q9HNU8;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-hydroxyphenyl transferase;
DE EC=2.5.1.147;
DE AltName: Full=FO synthase subunit 2;
GN Name=cofH; OrderedLocusNames=VNG_1938C;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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.
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;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F0 biosynthesis.
CC -!- SUBUNIT: Consists of two subunits, CofG and CofH. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. CofH family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG20122.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE004437; AAG20122.1; ALT_INIT; Genomic_DNA.
DR PIR; F84344; F84344.
DR RefSeq; WP_010903422.1; NC_002607.1.
DR AlphaFoldDB; Q9HNU8; -.
DR SMR; Q9HNU8; -.
DR STRING; 64091.VNG_1938C; -.
DR PaxDb; Q9HNU8; -.
DR EnsemblBacteria; AAG20122; AAG20122; VNG_1938C.
DR GeneID; 5954348; -.
DR GeneID; 62887280; -.
DR KEGG; hal:VNG_1938C; -.
DR PATRIC; fig|64091.14.peg.1481; -.
DR HOGENOM; CLU_040406_1_1_2; -.
DR InParanoid; Q9HNU8; -.
DR OrthoDB; 26917at2157; -.
DR UniPathway; UPA00072; -.
DR Proteomes; UP000000554; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR045567; CofH/MnqC-like_C.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR034405; F420.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR43076; PTHR43076; 1.
DR Pfam; PF19288; CofH_C; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 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..453
FT /note="5-amino-6-(D-ribitylamino)uracil--L-tyrosine 4-
FT hydroxyphenyl transferase"
FT /id="PRO_0000141715"
FT DOMAIN 74..344
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT REGION 418..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 88
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
SQ SEQUENCE 453 AA; 48620 MW; 5A8357FDACF3572F CRC64;
MTDASALDFD VVPSTDQSFE NALANARDGR RLTVADGIEL ITTGTDTDGI DPRRKELVLE
AADRRRADVV GDDVTFVANL NNNVTTACNT GCLFCNFKDT AHRFETEHEA AHGGFTKTPA
ESKATVADAI QRGVSEVTSV SGLHPAFGLN EAHRDALDPD DPDHNYKPPE AYDTDPTTYA
AQIAAMSEAG AHVHSITPEE AHHAQRGVSW GYDEVYETLA DAGLDTVPGT AAEILVDEVR
DVICPGKMTT DEWVAAMEAA ADAGLGTTAT IMYGHVENAA HRIHHLDVIR ALQDRTHNIT
EFVPLSFIHE QTPLYERGVV DGGASDAEDE LMIAVSRLFL DNIDHIQSSW VKFGDAKGLA
LLNCGADDFM GTILSEEITK RAGGQHGEFR SVADYAEMIS AIGRTPVERS TDYTTRHVIN
PDADTIGPHV GPNADGTPLV SERAGTPPHS AGD
