ID G2PW99_9FIRM Unreviewed; 375 AA.
AC G2PW99;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Dihydropteroate synthase {ECO:0000256|ARBA:ARBA00016919};
DE EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458};
DE AltName: Full=Dihydropteroate pyrophosphorylase {ECO:0000256|ARBA:ARBA00030193};
GN ORFNames=Calla_2137 {ECO:0000313|EMBL:AEM74700.1};
OS Caldicellulosiruptor acetigenus 6A.
OC Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales;
OC Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX NCBI_TaxID=632516 {ECO:0000313|EMBL:AEM74700.1, ECO:0000313|Proteomes:UP000009257};
RN [1] {ECO:0000313|EMBL:AEM74700.1, ECO:0000313|Proteomes:UP000009257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6A {ECO:0000313|EMBL:AEM74700.1,
RC ECO:0000313|Proteomes:UP000009257};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Blumer-Schuette S.E.,
RA Kelly R.M., Woyke T.;
RT "Complete sequence of Caldicellulosiruptor lactoaceticus 6A.";
RL Submitted (AUG-2011) 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}.
CC -!- SIMILARITY: Belongs to the DHPS family.
CC {ECO:0000256|ARBA:ARBA00009503}.
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DR EMBL; CP003001; AEM74700.1; -; Genomic_DNA.
DR RefSeq; WP_014043184.1; NC_015949.1.
DR AlphaFoldDB; G2PW99; -.
DR KEGG; clc:Calla_2137; -.
DR HOGENOM; CLU_008023_0_2_9; -.
DR UniPathway; UPA00077; UER00156.
DR Proteomes; UP000009257; 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 GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00739; DHPS; 1.
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 3: Inferred from homology;
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 113..367
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 375 AA; 42372 MW; E0F9AABD4B530AB2 CRC64;
MRLISKDANI KRILYQKGFD EKDILEFEKE ANSIILRFDD VKNPSRFIQL LSNLGYFTIS
NGSMCFATTS LNSLEKTRCV LAEEGIQCSF DVDLTISQRY LLAKDKKLSL LKTNVMGIIN
VTPDSFYEGS RVQVEKVTQR ALQMIQDGAD VLDIGGESTR PFSEPVPEEE ELKRVIPAIE
AIREVDKNIP ISIDTYKSRV AQKAIEAGAD IINDISGGTF DKEMFYVAAH YNVPIVIMHI
KGTPKDMQKN PYYEDVIEEI LQFFEQRIEQ ALKAGVKLEN IILDPGIGFG KRLEDNLEIL
RRCEEFKVLG RPILIGASRK SVIGHVLGNL PPEERLEGTL AISVICAQKK IEFVRVHDVK
ENKRAILMTQ AIFQS
//
