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Database: UniProt
Entry: A0A0E3NXY4_9EURY
LinkDB: A0A0E3NXY4_9EURY
Original site: A0A0E3NXY4_9EURY 
ID   A0A0E3NXY4_9EURY        Unreviewed;       388 AA.
AC   A0A0E3NXY4;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458};
DE            EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458};
GN   ORFNames=MSMTP_2358 {ECO:0000313|EMBL:AKB25827.1};
OS   Methanosarcina sp. MTP4.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=1434100 {ECO:0000313|EMBL:AKB25827.1, ECO:0000313|Proteomes:UP000033049};
RN   [1] {ECO:0000313|EMBL:AKB25827.1, ECO:0000313|Proteomes:UP000033049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MTP4 {ECO:0000313|EMBL:AKB25827.1,
RC   ECO:0000313|Proteomes:UP000033049};
RA   Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA   Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT   "Methanogenic archaea and the global carbon cycle.";
RL   Submitted (JUL-2014) 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; CP009505; AKB25827.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E3NXY4; -.
DR   STRING; 1434100.MSMTP_2358; -.
DR   KEGG; metm:MSMTP_2358; -.
DR   PATRIC; fig|1434100.4.peg.3146; -.
DR   HOGENOM; CLU_008023_3_0_2; -.
DR   Proteomes; UP000033049; Chromosome.
DR   GO; GO:0004156; F:dihydropteroate synthase activity; IEA:InterPro.
DR   GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IEA:InterPro.
DR   CDD; cd00739; DHPS; 1.
DR   Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1.
DR   InterPro; IPR045031; DHP_synth.
DR   InterPro; IPR006390; DHP_synth_dom.
DR   InterPro; IPR011005; Dihydropteroate_synth-like.
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; 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:UP000033049};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..246
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50972"
SQ   SEQUENCE   388 AA;  42351 MW;  89ECF80E515327CB CRC64;
     MGVINLSPES FFKGSVVAPD SVLEIARKMV EDGATFLDVG ARSTWRFSEP ISKAEELKRL
     LPVLEVLDGN VDAVISVDTM FSEIAEETLR RGADLVNDVS GFTIDPDMIR VVADHGCPAV
     VMASEKVPGD PLGMDAIISE LDSIIRTAEA GGIDPNGLIL DPAIGRWTEE KLSFYDFETL
     DDFDRLKIFE KPLLAALSRK SFIGEVLEKP APERLYGSLA AAAIAVYKGA HIIRTHDVPE
     TVDAVKVAGA LRSRPSLVKE ARYEVSVVEI KTPQDASLVM RKLGATGVGS QVMRDKSVHL
     VLRIRNLTTT EALIIKQELL ARGGDAALTR DAVSHETETT DVLVMGTLLQ LERLARKLEG
     QARSLPLIAG MLRECIANRS DLDYRYSR
//
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