ID A0A077HJN1_9CORY Unreviewed; 283 AA.
AC A0A077HJN1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Dihydropteroate synthase {ECO:0000256|RuleBase:RU361205};
DE Short=DHPS {ECO:0000256|RuleBase:RU361205};
DE EC=2.5.1.15 {ECO:0000256|RuleBase:RU361205};
DE AltName: Full=Dihydropteroate pyrophosphorylase {ECO:0000256|RuleBase:RU361205};
GN ORFNames=CUREI_04705 {ECO:0000313|EMBL:AIL96686.1};
OS Corynebacterium ureicelerivorans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=401472 {ECO:0000313|EMBL:AIL96686.1, ECO:0000313|Proteomes:UP000028939};
RN [1] {ECO:0000313|EMBL:AIL96686.1, ECO:0000313|Proteomes:UP000028939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMMIB RIV-2301 {ECO:0000313|EMBL:AIL96686.1,
RC ECO:0000313|Proteomes:UP000028939};
RA Tippelt A., Albersmeier A., Brinkrolf K., Ruckert C., Tauch A.;
RT "Complete genome sequence of Corynebacterium ureicelerivorans DSM 45051, a
RT lipophilic and urea-splitting isolate from a blood culture of a septicaemia
RT patient.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with
CC 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-
CC dihydropteroate (H2Pte), the immediate precursor of folate derivatives.
CC {ECO:0000256|RuleBase:RU361205}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU361205};
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|RuleBase:RU361205}.
CC -!- SIMILARITY: Belongs to the DHPS family.
CC {ECO:0000256|RuleBase:RU361205}.
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DR EMBL; CP009215; AIL96686.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077HJN1; -.
DR STRING; 401472.CUREI_04705; -.
DR KEGG; cuv:CUREI_04705; -.
DR HOGENOM; CLU_008023_0_0_11; -.
DR UniPathway; UPA00077; UER00156.
DR Proteomes; UP000028939; 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:SF8; INACTIVE DIHYDROPTEROATE SYNTHASE 2; 1.
DR Pfam; PF00809; Pterin_bind; 1.
DR SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR PROSITE; PS00792; DHPS_1; 1.
DR PROSITE; PS00793; DHPS_2; 1.
DR PROSITE; PS50972; PTERIN_BINDING; 1.
PE 3: Inferred from homology;
KW Folate biosynthesis {ECO:0000256|RuleBase:RU361205};
KW Magnesium {ECO:0000256|RuleBase:RU361205};
KW Metal-binding {ECO:0000256|RuleBase:RU361205};
KW Reference proteome {ECO:0000313|Proteomes:UP000028939};
KW Transferase {ECO:0000256|RuleBase:RU361205}.
FT DOMAIN 6..264
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 283 AA; 29823 MW; 0120A07ABB6ACF9F CRC64;
MSRPLAQVMA IVNRTPDSFY DKGATFAAEK ALERIDAAVA AGATIIDIGG VKAGPGDDVS
VAAEIERVVP TIELARQRHP GVTISVDTWR APVAEAAINA GADLVNDTWA GFDPELVEVA
GAHGVGYVCS HTGGVTPRTR PHRVHYDDVV ADVIAETTAL AERAVHLGVP EEKIFIDPTH
DFGKNTYHGL ELLRRVDELV ATGWPVLMAL SNKDFVGETV NRGIGGSDVA ERVPGTLAAT
AWAAAHGVAA FRVHEVEATL DVIRMTAAIA GDMAPLYTVR GLA
//
