ID A0A238WJD9_HALVU Unreviewed; 864 AA.
AC A0A238WJD9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458};
DE EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458};
GN ORFNames=SAMN06264855_107149 {ECO:0000313|EMBL:SNR45789.1};
OS Halorubrum vacuolatum (Natronobacterium vacuolatum).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=63740 {ECO:0000313|EMBL:SNR45789.1, ECO:0000313|Proteomes:UP000198397};
RN [1] {ECO:0000313|EMBL:SNR45789.1, ECO:0000313|Proteomes:UP000198397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8800 {ECO:0000313|EMBL:SNR45789.1,
RC ECO:0000313|Proteomes:UP000198397};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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; FZNQ01000007; SNR45789.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238WJD9; -.
DR OrthoDB; 75177at2157; -.
DR Proteomes; UP000198397; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004156; F:dihydropteroate synthase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
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 Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR InterPro; IPR045031; DHP_synth-like.
DR InterPro; IPR006390; DHP_synth_dom.
DR InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR InterPro; IPR001645; Folylpolyglutamate_synth.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR004101; Mur_ligase_C.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR InterPro; IPR000489; Pterin-binding_dom.
DR NCBIfam; TIGR01496; DHPS; 1.
DR NCBIfam; TIGR01499; folC; 1.
DR PANTHER; PTHR20941; FOLATE SYNTHESIS PROTEINS; 1.
DR PANTHER; PTHR20941:SF1; FOLIC ACID SYNTHESIS PROTEIN FOL1; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR Pfam; PF00809; Pterin_bind; 1.
DR SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR PROSITE; PS00792; DHPS_1; 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:UP000198397};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 594..850
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 864 AA; 89545 MW; 39F4F472D3131AEC CRC64;
MQYHEAVRFL FDLRRFSMRP GTEGVEALLE HLDHPEHGVP FVQIAGSNGK GSTARLVESI
LREAGLSVGL YTSPHLESLT ERVHVDGLPI TRSAIADFIG RVRPWLIDRA AAGEPLTLFE
VVTAMAIDEF ARRNVDVAVL EVGLGGEYDA TSAVDPVATA VTNVSLEHTS VLGDSVAEIA
RTKSRIATDG TPLVTACDGE ALRVLREVAA DAGAPVSTVV GPGVDGEGTD SPALRATYEG
RVSPTDAAVT LSGEVTGTYR IPLVGTHQAT NAAVAVALAR RTVDALGGNA ADSDGRVDER
AVADGLARAT WPGRFEVIST DPLVILDGAH NPAACETVAG TLAEYDYDAL HLVYAAMHDK
DHAGTIGALP TAASVVTCRT NTDRAEDPAV LAAAARRAGF PDVTAGEGVA DALDRALDRA
DADDCVLLFG SLYAVAEARA AKTRTVTPLT VRDATDAAGV LERAAAPIDG RSGDGETPSA
AAEAIDTRVL TCQLRGEQAR YIRGELRALG GTAVIGGAGA AGGELVPVVL SATRATFRAL
CDRLERAGRN ATPPVDGLPG IAADLRDRLL THSIDDDDGN AAGSIDPYPW TDGTAVMGVL
NVTPDSFYDG GVHEALDDAV AGAKRMVEAG VDVIDVGGES TRPGADPVPA DAEIDRVVPV
LEALHDVAAV ADGDVLLSID TRKPTVAEAA LAAGADIIND VTGLEDPRMR EVVADAGCPV
VLMHSTDAPV DPTADPEYDD VVTDVIAILE ERLRLAEIAG IDRERVIVDP GIGFGKTAAE
SFALLGRLPE FAALDCPVLV GHSHKSLFGA IGRDPDDREH ATVAATALAA ARGADLVRVH
DVAENRAAVD VARAVGDPNA VDPE
//
