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Entry: D5E8C0_METMS
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ID   D5E8C0_METMS            Unreviewed;       411 AA.
AC   D5E8C0;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458};
DE            EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458};
GN   OrderedLocusNames=Mmah_1913 {ECO:0000313|EMBL:ADE37408.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE37408.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE37408.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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; CP001994; ADE37408.1; -; Genomic_DNA.
DR   RefSeq; WP_013038350.1; NC_014002.1.
DR   AlphaFoldDB; D5E8C0; -.
DR   STRING; 547558.Mmah_1913; -.
DR   GeneID; 8984100; -.
DR   KEGG; mmh:Mmah_1913; -.
DR   HOGENOM; CLU_008023_3_0_2; -.
DR   OrthoDB; 371861at2157; -.
DR   Proteomes; UP000001059; Chromosome.
DR   GO; GO:0004156; F:dihydropteroate synthase activity; IEA:UniProtKB-EC.
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:UP000001059};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADE37408.1}.
FT   DOMAIN          18..266
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50972"
SQ   SEQUENCE   411 AA;  44947 MW;  8610449BDE610589 CRC64;
     MVVDVDICGL KVGDNHPVRL MGVLNLSHES FYKGSVVRED SLIDAASAML EEGANVLDIG
     GRSTWPLAEP LSKELERKRL LPAIDALAGN VDAVLSVDTV FADIADQCLD RGAGIVNDVS
     GFMTDENMVD VVADHECPAV VMASRQVPGD VLGMDEVMDS LEAIIELCEG KGIDTDQLIL
     DPAIGKWVPE KDPIYDFETF DRFERLQTFG KPVLAALSRK SFIGEVLNKP AAERLYGSLA
     ATAIAVHKGA HIIRTHDVAA TTDAVRIAEA IRGRIPCQKA DERQVRMLEI TDPDDSVRVM
     KSLGVTSTGA QVMKNKSVMF NLLVCNITTT EALIIKQEIL ARGGDACLER NAVSHETEYT
     DLVVMGTLLQ LKKLVAKLQD QARGLPQIAT MLDTVLDEYY DVEYRYSFRN V
//
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