ID I3ASF4_BIFLN Unreviewed; 296 AA.
AC I3ASF4;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 30.
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:EIJ22047.1};
GN ORFNames=HMPREF1314_1742 {ECO:0000313|EMBL:EIJ22047.1};
OS Bifidobacterium longum subsp. longum 35B.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1161904 {ECO:0000313|EMBL:EIJ22047.1, ECO:0000313|Proteomes:UP000004446};
RN [1] {ECO:0000313|EMBL:EIJ22047.1, ECO:0000313|Proteomes:UP000004446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35B {ECO:0000313|EMBL:EIJ22047.1};
RX PubMed=23682142;
RA Shkoporov A.N., Efimov B.A., Khokhlova E.V., Chaplin A.V., Kafarskaya L.I.,
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Sutton G., Weibel D.B.,
RA Nelson K.E., Smeianov V.V.;
RT "Draft Genome Sequences of Two Pairs of Human Intestinal Bifidobacterium
RT longum subsp. longum Strains, 44B and 1-6B and 35B and 2-2B, Consecutively
RT Isolated from Two Children after a 5-Year Time Period.";
RL Genome Announc. 1:E00234-E00213(2013).
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}.
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:EIJ22047.1}.
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DR EMBL; AJTI01000125; EIJ22047.1; -; Genomic_DNA.
DR AlphaFoldDB; I3ASF4; -.
DR PATRIC; fig|1161904.3.peg.1959; -.
DR Proteomes; UP000004446; Unassembled WGS sequence.
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; 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:EIJ22047.1}.
FT DOMAIN 18..287
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 296 AA; 31123 MW; C17ADC5B9C8CEDA7 CRC64;
MEGEPMTDLR ALRDSSRTMV MGVLNITEDS SSDGGLWLDP AKAAQHGRDM MAAGADIIDI
GAESTRPGAK RVSEADELAR ITGAVKTLIP AGAILSIDTT RASVAAAALS EGAQIINDVS
GGTLDAELPQ VVADHDCLYI VQHWRGWLAG SKGANPDQDT SVYEHGVLTD VHDELMRQVD
GVLAAGVKPE RIIIDPGLGF SKPGIEHNLP LLTGLETFRA TGYPVLIGQS RKRFISAMLT
EAGAAGADGP IMAQRDDVTA ALSALSAEHG AWAVRVHDVA KSRAAVIAGN TWREYA
//
