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Database: UniProt
Entry: A0A2K5ANZ9_9ARCH
LinkDB: A0A2K5ANZ9_9ARCH
Original site: A0A2K5ANZ9_9ARCH 
ID   A0A2K5ANZ9_9ARCH        Unreviewed;       276 AA.
AC   A0A2K5ANZ9;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458};
DE            EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458};
GN   ORFNames=NCAV_0157 {ECO:0000313|EMBL:SPC33357.1};
OS   Candidatus Nitrosocaldus cavascurensis.
OC   Archaea; Nitrososphaerota; Nitrososphaeria; Candidatus Nitrosocaldales;
OC   Candidatus Nitrosocaldaceae; Candidatus Nitrosocaldus.
OX   NCBI_TaxID=2058097 {ECO:0000313|EMBL:SPC33357.1, ECO:0000313|Proteomes:UP000236248};
RN   [1] {ECO:0000313|Proteomes:UP000236248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCU2 {ECO:0000313|Proteomes:UP000236248};
RA   Kerou L M.;
RL   Submitted (JAN-2018) 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; LT981265; SPC33357.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K5ANZ9; -.
DR   KEGG; ncv:NCAV_0157; -.
DR   Proteomes; UP000236248; Chromosome ncav.
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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          2..265
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50972"
SQ   SEQUENCE   276 AA;  30198 MW;  C4231219BA06ABD3 CRC64;
     MVRIMGIVNV SPESFYKGSV KVTEEDIART VASMEEYGAS IVDVGAMSTA PYLDTVVPVE
     EEIARLKHAI KVIKDSCSLT ISVDTPRAKT ADAALNAGAT VINDVTGLKY DPDMARTAKE
     HSASVIVSAY SKHKVQGDVI ATTLELLKES IDVAVDAGID EDKIIVDPAI GFFREHGRHE
     FFTKLEGMTW LERDLAVVRR LRELKVLGKE VCVSPSRKSF IGRILNLDKP EDRLYGSLAV
     EAVCIINGAD IIRTHNVKES IQVARVVEAI MGRCGW
//
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