DHPSL_METJA
ID DHPSL_METJA Reviewed; 294 AA.
AC Q57749;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase;
DE EC=2.5.1.105;
GN OrderedLocusNames=MJ0301;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION AS A PTEROATE SYNTHASE, CATALYTIC ACTIVITY, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=10426953; DOI=10.1038/11525;
RA Xu H., Aurora R., Rose G.D., White R.H.;
RT "Identifying two ancient enzymes in Archaea using predicted secondary
RT structure alignment.";
RL Nat. Struct. Biol. 6:750-754(1999).
CC -!- FUNCTION: Catalyzes the condensation of 6-hydroxymethyl-7,8-
CC dihydropterin pyrophosphate (DHPP) with 4-(beta-D-ribofuranosyl)-
CC aminobenzene-5'-phosphate (beta-RFA-P) to form 7,8-dihydropterin-6-
CC methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate, a precursor
CC in the biosynthesis of 5,6,7,8-tetrahydromethanopterin (H4MPT). To a
CC lesser extent, is able to condense beta-RFA-P with another arylamine,
CC 1-(4-aminophenyl)-1-deoxy-D-ribitol (APDR), to form 7,8-dihydropterin-
CC 6-methyl-1-(4-aminophenyl)-1-deoxy-D-ribitol. Dephosphorylated beta-
CC RFA-P is not a substrate. {ECO:0000269|PubMed:10426953}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7,8-dihydropterin-6-yl)methyl diphosphate + 4-(beta-D-
CC ribofuranosyl)aminobenzene 5'-phosphate = diphosphate + N-[(7,8-
CC dihydropterin-6-yl)methyl]-4-(beta-D-ribofuranosyl)aniline 5'-
CC phosphate; Xref=Rhea:RHEA:35951, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:72778, ChEBI:CHEBI:72950, ChEBI:CHEBI:72951;
CC EC=2.5.1.105; Evidence={ECO:0000269|PubMed:10426953};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin
CC biosynthesis.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC {ECO:0000305}.
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DR EMBL; L77117; AAB98288.1; -; Genomic_DNA.
DR PIR; F64337; F64337.
DR RefSeq; WP_010869799.1; NC_000909.1.
DR AlphaFoldDB; Q57749; -.
DR SMR; Q57749; -.
DR STRING; 243232.MJ_0301; -.
DR EnsemblBacteria; AAB98288; AAB98288; MJ_0301.
DR GeneID; 1451156; -.
DR KEGG; mja:MJ_0301; -.
DR eggNOG; arCOG00503; Archaea.
DR HOGENOM; CLU_036012_0_0_2; -.
DR InParanoid; Q57749; -.
DR OMA; CSGWRAK; -.
DR OrthoDB; 73329at2157; -.
DR PhylomeDB; Q57749; -.
DR BioCyc; MetaCyc:MON-14570; -.
DR BRENDA; 2.5.1.105; 3260.
DR UniPathway; UPA00065; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0102041; F:7,8-dihydropterin-6-yl-methyl-4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate synthase; IEA:UniProtKB-EC.
DR GO; GO:0102638; F:[1-(2-amino-7-methyl-4-oxo-7,8-dihydro-3H-pteridin-6-yl)]ethyl-4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IBA:GO_Central.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IDA:UniProtKB.
DR GO; GO:1901285; P:5,6,7,8-tetrahydromethanopterin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IDA:UniProtKB.
DR CDD; cd07713; DHPS-like_MBL-fold; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR041712; DHPS-like_MBL-fold.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW Magnesium; Metal-binding; Reference proteome; Transferase.
FT CHAIN 1..294
FT /note="7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-
FT aminobenzene-5'-phosphate synthase"
FT /id="PRO_0000106783"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 294 AA; 33076 MW; 0FC92953FF9E005A CRC64;
MLMNIGKVDN IKIYTLAEDY AGYNSPFWSQ HGLSFLIEVE SNGIKKRILF DTATYAEPIL
FNMKLLNINP KSIDMIILSH NHFDHTGGLF GIMKEINKEI PIFAHPNIFK VSFATEPEFM
LAGTLNKTLK EDIEKLGGRW VLSRDPIRLM PGIFTLGEIE DEEKINFEKK PTIGLYKLEN
GRVVLDNVED EIGLAIVTEK GLIIVSGCSH PGIVSMVKKS IKISGINKVY AVIGGFHLID
ADNERIVSTI KALKKLGVKK ICTGHCTGFK AENMFMEEFK EDFERLHAGK IIKF
