ID E4NT22_HALBP Unreviewed; 388 AA.
AC E4NT22;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458};
DE EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458};
GN OrderedLocusNames=Hbor_14350 {ECO:0000313|EMBL:ADQ67015.1};
GN ORFNames=C499_04626 {ECO:0000313|EMBL:ELY29806.1};
OS Halogeometricum borinquense (strain ATCC 700274 / DSM 11551 / JCM 10706 /
OS KCTC 4070 / PR3).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halogeometricum.
OX NCBI_TaxID=469382 {ECO:0000313|EMBL:ADQ67015.1, ECO:0000313|Proteomes:UP000006663};
RN [1] {ECO:0000313|EMBL:ADQ67015.1, ECO:0000313|Proteomes:UP000006663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700274 / DSM 11551 / JCM 10706 / KCTC 4070 / PR3
RC {ECO:0000313|Proteomes:UP000006663}, and PR 3
RC {ECO:0000313|EMBL:ADQ67015.1};
RX PubMed=21304651; DOI=10.4056/sigs.23264;
RA Malfatti S., Tindall B.J., Schneider S., Fahnrich R., Lapidus A.,
RA Labuttii K., Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Anderson I.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA D'haeseleer P., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Chain P.;
RT "Complete genome sequence of Halogeometricum borinquense type strain
RT (PR3).";
RL Stand. Genomic Sci. 1:150-159(2009).
RN [2] {ECO:0000313|EMBL:ELY29806.1, ECO:0000313|Proteomes:UP000011585}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11551 {ECO:0000313|EMBL:ELY29806.1,
RC ECO:0000313|Proteomes:UP000011585};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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; CP001690; ADQ67015.1; -; Genomic_DNA.
DR EMBL; AOHT01000013; ELY29806.1; -; Genomic_DNA.
DR RefSeq; WP_006054245.1; NZ_AOHT01000013.1.
DR AlphaFoldDB; E4NT22; -.
DR STRING; 469382.Hbor_14350; -.
DR GeneID; 9993254; -.
DR KEGG; hbo:Hbor_14350; -.
DR PATRIC; fig|469382.19.peg.907; -.
DR eggNOG; arCOG02817; Archaea.
DR HOGENOM; CLU_008023_3_0_2; -.
DR OrthoDB; 371861at2157; -.
DR Proteomes; UP000006663; Chromosome.
DR Proteomes; UP000011585; 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 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; 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:UP000006663};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADQ67015.1}.
FT DOMAIN 17..262
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 388 AA; 41762 MW; 94EA40524A53971C CRC64;
MRTVDAAGLE IGDDHPPRIM GVLNVSKESP YEPSVFNDAG EAAKYVDTAL IDEGADIVDV
GLESANKRFE VLSAEEELDR LDTAVEVLES VSGDAVFSIE TRYHEVADEA LSRGFDMVND
ICGFADPEMP TVCTDHDAAV AKMASPPDLE RPGAIEEVDD IYDALAQNGF TDKTIVDPAF
GGWSEAKTLE HDRETLRRLR EFRGYGRPIL VSINRKNFLR EVAGRDTEEA LPVSLAATSM
AVERGAHVIR THDVAETRDA ALIGKEFARH RTRKSGDVTV EELDVTTPRE VERHLDRLGV
ESPASIATEA VVRVFELDGL SDEDVRTLAA AAGDAGATVA RGTTADGADS HCVLLLGTAR
ALCETVAFSE GESESLATAL HSVENGVL
//
