ID A0A0W0GGE2_9CHLR Unreviewed; 465 AA.
AC A0A0W0GGE2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Dihydropteroate synthase/2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase {ECO:0000313|EMBL:KTB47637.1};
GN ORFNames=DEALK_04820 {ECO:0000313|EMBL:KTB47637.1};
OS Dehalogenimonas alkenigignens.
OC Bacteria; Chloroflexota; Dehalococcoidia; Dehalogenimonas.
OX NCBI_TaxID=1217799 {ECO:0000313|EMBL:KTB47637.1, ECO:0000313|Proteomes:UP000053947};
RN [1] {ECO:0000313|EMBL:KTB47637.1, ECO:0000313|Proteomes:UP000053947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP3-3 {ECO:0000313|EMBL:KTB47637.1,
RC ECO:0000313|Proteomes:UP000053947};
RA Key T.A., Richmond D.P., Bowman K.S., Cho Y.-J., Chun J., da Costa M.S.,
RA Rainey F.A., Moe W.M.;
RT "Genome sequence of the organohalide-respiring Dehalogenimonas
RT alkenigignens type strain (IP3-3T).";
RL Submitted (JUN-2015) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-
CC 6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841,
CC ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000198};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-
CC 4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-
CC dihydroneopterin triphosphate: step 4/4.
CC {ECO:0000256|ARBA:ARBA00005051}.
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: In the C-terminal section; belongs to the DHPS family.
CC {ECO:0000256|ARBA:ARBA00009951}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KTB47637.1}.
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DR EMBL; LFDV01000002; KTB47637.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0GGE2; -.
DR STRING; 1217799.DEALK_04820; -.
DR PATRIC; fig|1217799.6.peg.499; -.
DR UniPathway; UPA00077; UER00155.
DR Proteomes; UP000053947; Unassembled WGS sequence.
DR GO; GO:0003848; F:2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004156; F:dihydropteroate synthase activity; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00739; DHPS; 1.
DR CDD; cd00483; HPPK; 1.
DR Gene3D; 3.30.70.560; 7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK; 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; IPR000550; Hppk.
DR InterPro; IPR035907; Hppk_sf.
DR InterPro; IPR000489; Pterin-binding_dom.
DR NCBIfam; TIGR01496; DHPS; 1.
DR NCBIfam; TIGR01498; folK; 1.
DR PANTHER; PTHR20941; FOLATE SYNTHESIS PROTEINS; 1.
DR PANTHER; PTHR20941:SF1; FOLIC ACID SYNTHESIS PROTEIN FOL1; 1.
DR Pfam; PF01288; HPPK; 1.
DR Pfam; PF00809; Pterin_bind; 1.
DR SUPFAM; SSF55083; 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KTB47637.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053947};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 47..294
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 465 AA; 49791 MW; 29C6906382BA68BC CRC64;
MEFKTPRPGR SLARGQPHGY HYEVSFNIPL AQPTRIGSRT FRWGRRTYVM GILNVTPDSF
SGDGLGGDIG AAIAQAERMA AEGADIIDVG GESTRPGAPE VSAAEEISRV VPVIERLKAA
IDLPVSIDSY KAEVAEAAVT AGASLLNDVW GLKRDARLAD VAARRGLPIV ISSSQRDAPA
ADIMTAVLDS LRWAIGRAAE AGVARENIIL DPGFGFGKTV EQNVEALRRL DELRAFGRPV
LLGTSRKSTI GKVLGDAPPQ ERLFGTVATT AIGIMNGADI VRVHDVKENV QAARMADAVA
RGVTVYLGLG SNLGDRKRNL ALAAEAVSRD LHVNQLSPVY ETEPWNVAPQ PRFLNMAIEA
QTTLSPSDLL DYVKNLERML GRAAAGPGQP RVIDIDILLY GDQVLDTPAL TLPHPRLAQR
AFNLVPLNDL DPELKHPATG RTAAEMLSAL GQIRGVAPYP ENTPD
//
