ID A0A075WTT5_9BACT Unreviewed; 284 AA.
AC A0A075WTT5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458};
DE EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458};
GN ORFNames=HL41_02750 {ECO:0000313|EMBL:AIH03798.1};
OS Thermodesulfobacterium commune DSM 2178.
OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC Thermodesulfobacteriales; Thermodesulfobacteriaceae;
OC Thermodesulfobacterium.
OX NCBI_TaxID=289377 {ECO:0000313|EMBL:AIH03798.1, ECO:0000313|Proteomes:UP000028481};
RN [1] {ECO:0000313|EMBL:AIH03798.1, ECO:0000313|Proteomes:UP000028481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2178 {ECO:0000313|EMBL:AIH03798.1,
RC ECO:0000313|Proteomes:UP000028481};
RX PubMed=25635017;
RA Bhatnagar S., Badger J.H., Madupu R., Khouri H.M., O'Connor E.M.,
RA Robb F.T., Ward N.L., Eisen J.A.;
RT "Genome Sequence of a Sulfate-Reducing Thermophilic Bacterium,
RT Thermodesulfobacterium commune DSM 2178T (Phylum Thermodesulfobacteria).";
RL Genome Announc. 3:0-0(2015).
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; CP008796; AIH03798.1; -; Genomic_DNA.
DR RefSeq; WP_038061209.1; NZ_JQLF01000009.1.
DR AlphaFoldDB; A0A075WTT5; -.
DR STRING; 289377.HL41_02750; -.
DR PaxDb; 289377-HL41_02750; -.
DR KEGG; tcm:HL41_02750; -.
DR eggNOG; COG0294; Bacteria.
DR HOGENOM; CLU_008023_0_2_0; -.
DR OrthoDB; 9811744at2; -.
DR Proteomes; UP000028481; 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 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 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:UP000028481};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 18..273
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 284 AA; 31926 MW; A1BA15075118F091 CRC64;
MLSPLKIGSK IFDWQACPYF MGILNVTPDS FSDGGKFFGL KEAVLRAKEL IEEGADIIDI
GGESTRPFSE PVSEEEELKR VVPVVKAIRE EFPDVVISVD TYKSRVAEEA LKAGASMIND
ISAGCFDQRM VEVVKDFDCP YVIMHIKGTP KTMQENPQYK DVVKEVKEFL QNRIEFLVKK
GISVEKIIVD PGLGFGKTFE HNLEILKRLD EFYSLGRPVL LGHSRKSFIG KVLNKPNPLD
REGGTIGFSV WASLRGVHFL RVHRVDLNKD AVIMFKFLTQ QKGG
//
