ID A4TVW2_9PROT Unreviewed; 359 AA.
AC A4TVW2;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458};
DE EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458};
GN Name=folP {ECO:0000313|EMBL:CAM74769.1};
GN ORFNames=MGR_1803 {ECO:0000313|EMBL:CAM74769.1};
OS Magnetospirillum gryphiswaldense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=55518 {ECO:0000313|EMBL:CAM74769.1};
RN [1] {ECO:0000313|EMBL:CAM74769.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MSR-1 {ECO:0000313|EMBL:CAM74769.1};
RX PubMed=17449609; DOI=10.1128/JB.00119-07;
RA Richter M., Kube M., Bazylinski D.A., Lombardot T., Gloeckner F.O.,
RA Reinhardt R., Schueler D.;
RT "Comparative genome analysis of four magnetotactic bacteria reveals a
RT complex set of group-specific genes implicated in magnetosome
RT biomineralization and function.";
RL J. Bacteriol. 189:4899-4910(2007).
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; CU459003; CAM74769.1; -; Genomic_DNA.
DR AlphaFoldDB; A4TVW2; -.
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 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; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAM74769.1}.
FT DOMAIN 98..350
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 359 AA; 37483 MW; 37A3F6424760BEB7 CRC64;
MHAPRVHVLP SGIVAGEAAA AAIIGGHGWP LADGKLAFTS AGIVWAEGGQ NWIGMAPYAE
LVAWAEAEGE DMARHIGQVV QRIGARRAEW AGLSLDRPRI MGIVNATPDS FSDGGRNLVA
QTAIANALAM VEAGADIIDV GGESTRPGAE PVSIDEEIRR VEPIIRALAE WKVTVSVDTR
HAPVMQAALA AGARIINDVT ALEGPGSLEV AVQSGAAVIL MHMQGQPQTM QADPRYTCAP
LDVYDYLASR IAVCEAAGLP RSRIMADPGI GFGKNAAHNA QILATLPLLH GLGCPLLLAA
SRKTFVAHLS QGETPQHRLP GTLAAHLAGL NAGMQCLRVH DVAETVQAVK IWQAMSAAA
//
