ID G7WR57_METH6 Unreviewed; 409 AA.
AC G7WR57;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458};
DE EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458};
GN OrderedLocusNames=Mhar_2004 {ECO:0000313|EMBL:AET65360.1};
OS Methanothrix harundinacea (strain 6Ac) (Methanosaeta harundinacea).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanotrichales; Methanotrichaceae; Methanothrix.
OX NCBI_TaxID=1110509 {ECO:0000313|EMBL:AET65360.1, ECO:0000313|Proteomes:UP000005877};
RN [1] {ECO:0000313|EMBL:AET65360.1, ECO:0000313|Proteomes:UP000005877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6Ac {ECO:0000313|EMBL:AET65360.1,
RC ECO:0000313|Proteomes:UP000005877};
RX PubMed=22590603; DOI=10.1371/journal.pone.0036756;
RA Zhu J., Zheng H., Ai G., Zhang G., Liu D., Liu X., Dong X.;
RT "The genome characteristics and predicted function of methyl-group
RT oxidation pathway in the obligate aceticlastic methanogens, Methanosaeta
RT spp.";
RL PLoS ONE 7:E36756-E36756(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate =
CC 7,8-dihydropteroate + diphosphate; Xref=Rhea:RHEA:19949,
CC ChEBI:CHEBI:17836, ChEBI:CHEBI:17839, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:72950; EC=2.5.1.15;
CC Evidence={ECO:0000256|ARBA:ARBA00000012};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-
CC dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-
CC dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.
CC {ECO:0000256|ARBA:ARBA00004763}.
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DR EMBL; CP003117; AET65360.1; -; Genomic_DNA.
DR RefSeq; WP_014587536.1; NC_017527.1.
DR AlphaFoldDB; G7WR57; -.
DR STRING; 1110509.Mhar_2004; -.
DR GeneID; 12511177; -.
DR KEGG; mhi:Mhar_2004; -.
DR PATRIC; fig|1110509.7.peg.2224; -.
DR HOGENOM; CLU_008023_3_0_2; -.
DR Proteomes; UP000005877; Chromosome.
DR GO; GO:0004156; F:dihydropteroate synthase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1.
DR InterPro; IPR045031; DHP_synth-like.
DR InterPro; IPR006390; DHP_synth_dom.
DR InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR InterPro; IPR000489; Pterin-binding_dom.
DR NCBIfam; TIGR01496; DHPS; 1.
DR PANTHER; PTHR20941; FOLATE SYNTHESIS PROTEINS; 1.
DR PANTHER; PTHR20941:SF1; FOLIC ACID SYNTHESIS PROTEIN FOL1; 1.
DR Pfam; PF00809; Pterin_bind; 1.
DR SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR PROSITE; PS00793; DHPS_2; 1.
DR PROSITE; PS50972; PTERIN_BINDING; 1.
PE 4: Predicted;
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000005877};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 18..268
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 409 AA; 42940 MW; F69C161B302C5282 CRC64;
MTIEGFIGKI RVGDLHPVRV MGVINLSRES FYEESYAGID AVLGRALAFA EEGAEVLDLG
AVSTAPGSPS IPEEEERRRL FPALEAVLDG LGEEVVVSVD TQRASVADDA LSAGAGCIND
VSGLHDPAMA KTVADHDGSL IIMASKERPG DILDMRDIVA NLGERVRAAW EAGVAAEKVT
VDPGIGRWTP PKGPGHDLAI LDGLERLRVL KRPVMAAVSR KSFIGAVLER PSPSDRLPGS
LAAAAVAVYN GAHLVRTHDV AASLDVIRMA EAVRGRPAIA GAGGIEVEVF GHWGHPEDLH
QAFAGLGVGE GGAKALGGKG SFRALSLRGV TSPEAVVIKQ EMLARGGDAA IPTGALRCDP
GEMEVLVLGT AAQLRGLVKD LIDQPFRLPT ISGAIEEALD RLEDPKRYW
//
