ID R4V413_9GAMM Unreviewed; 261 AA.
AC R4V413;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458};
DE EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458};
GN ORFNames=SPISAL_03075 {ECO:0000313|EMBL:AGM40709.1};
OS Spiribacter salinus M19-40.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Spiribacter.
OX NCBI_TaxID=1260251 {ECO:0000313|EMBL:AGM40709.1, ECO:0000313|Proteomes:UP000017881};
RN [1] {ECO:0000313|EMBL:AGM40709.1, ECO:0000313|Proteomes:UP000017881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M19-40 {ECO:0000313|EMBL:AGM40709.1};
RX PubMed=23409269;
RA Leon M.J., Ghai R., Fernandez A.B., Sanchez-Porro C., Rodriguez-Valera F.,
RA Ventosa A.;
RT "Draft Genome of Spiribacter salinus M19-40, an Abundant
RT Gammaproteobacterium in Aquatic Hypersaline Environments.";
RL Genome Announc. 1:E00179-12(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}.
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DR EMBL; CP005963; AGM40709.1; -; Genomic_DNA.
DR AlphaFoldDB; R4V413; -.
DR KEGG; ssal:SPISAL_03075; -.
DR PATRIC; fig|1260251.3.peg.619; -.
DR eggNOG; COG0294; Bacteria.
DR HOGENOM; CLU_008023_0_3_6; -.
DR Proteomes; UP000017881; Chromosome.
DR GO; GO:0004156; F:dihydropteroate synthase activity; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000017881};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..250
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 261 AA; 27387 MW; 0E5755DFB639A81E CRC64;
MGILNVTPDS FSDGGVFVGA DQALAHARQM EADGAAIIDV GGESTRPGSR GVSVDEELSR
VIPVLEALHG EVSVPLSVDT SKPAVMRAAV DAGAGLINDV MALRRDGALA AARDLSVPVC
LMHMQGTPET MQDKPCYQHV VKEVVTFLLE RVEAAEAAGI ERCNLMLDPG FGFGKTDPHN
AELLKGLPKL VGHGLPVLAG LSRKSLVGRV LGRAMEERLA GSVALATMAT MHGARIIRAH
DVRETVDAVR LVNYVMAAQG A
//
