ID I3R3K1_HALMT Unreviewed; 816 AA.
AC I3R3K1;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
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:AFK18811.1};
GN OrderedLocusNames=HFX_1095 {ECO:0000313|EMBL:AFK18811.1};
GN ORFNames=BM92_03740 {ECO:0000313|EMBL:AHZ21822.1}, C439_05015
GN {ECO:0000313|EMBL:EMA03331.1}, E6P09_08500
GN {ECO:0000313|EMBL:QCQ75302.1};
OS Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
OS 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=523841 {ECO:0000313|EMBL:AFK18811.1, ECO:0000313|Proteomes:UP000006469};
RN [1] {ECO:0000313|EMBL:AFK18811.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.2087 {ECO:0000313|EMBL:AFK18811.1};
RX PubMed=22247127; DOI=10.1128/AEM.07114-11;
RA Cai S., Cai L., Liu H., Liu X., Han J., Zhou J., Xiang H.;
RT "Identification of the haloarchaeal phasin (PhaP) that functions in
RT polyhydroxyalkanoate accumulation and granule formation in Haloferax
RT mediterranei.";
RL Appl. Environ. Microbiol. 78:1946-1952(2012).
RN [2] {ECO:0000313|EMBL:AFK18811.1, ECO:0000313|Proteomes:UP000006469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
RC R-4 {ECO:0000313|Proteomes:UP000006469}, and CGMCC 1.2087
RC {ECO:0000313|EMBL:AFK18811.1};
RX PubMed=22843593; DOI=10.1128/JB.00880-12;
RA Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B., Chen Y.,
RA Zhou J., Hu S., Xiang H.;
RT "Complete genome sequence of the metabolically versatile halophilic
RT archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
RT hydroxyvalerate) producer.";
RL J. Bacteriol. 194:4463-4464(2012).
RN [3] {ECO:0000313|Proteomes:UP000011603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
RC R-4 {ECO:0000313|Proteomes:UP000011603};
RA Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A.,
RA Eisen J.A., Facciotti M.T.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:EMA03331.1, ECO:0000313|Proteomes:UP000011603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 {ECO:0000313|EMBL:EMA03331.1}, and ATCC 33500 / DSM
RC 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC {ECO:0000313|Proteomes:UP000011603};
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).
RN [5] {ECO:0000313|EMBL:AHZ21822.1, ECO:0000313|Proteomes:UP000027075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 {ECO:0000313|EMBL:AHZ21822.1}, and ATCC 33500 / DSM
RC 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC {ECO:0000313|Proteomes:UP000027075};
RA Bautista V.;
RT "Transcriptional profiles of Haloferax mediterranei on the basis of
RT nitrogen availability.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:AFK18811.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.2087;
RA Wang L., Yang H., Xiang H.;
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:QCQ75302.1, ECO:0000313|Proteomes:UP000299011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33500 {ECO:0000313|EMBL:QCQ75302.1}, and ATCC 33500 / DSM
RC 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC {ECO:0000313|Proteomes:UP000299011};
RA DasSarma S., DasSarma P., DasSarma S., Fomenkov A., Vincze T., Anton B.P.,
RA Roberts R.J.;
RT "Methylomes of two halophilic Archaea, Haloarcula marismortui and Haloferax
RT mediterranei.";
RL Submitted (APR-2019) 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 -!- 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001868; AFK18811.1; -; Genomic_DNA.
DR EMBL; CP007551; AHZ21822.1; -; Genomic_DNA.
DR EMBL; AOLO01000006; EMA03331.1; -; Genomic_DNA.
DR EMBL; CP039139; QCQ75302.1; -; Genomic_DNA.
DR RefSeq; WP_004572579.1; NZ_CP039139.1.
DR AlphaFoldDB; I3R3K1; -.
DR STRING; 523841.HFX_1095; -.
DR PaxDb; 523841-HFX_1095; -.
DR GeneID; 40156451; -.
DR KEGG; hme:HFX_1095; -.
DR PATRIC; fig|523841.21.peg.1014; -.
DR eggNOG; arCOG02817; Archaea.
DR HOGENOM; CLU_017222_0_0_2; -.
DR OrthoDB; 75177at2157; -.
DR Proteomes; UP000006469; Chromosome.
DR Proteomes; UP000011603; Unassembled WGS sequence.
DR Proteomes; UP000027075; Chromosome.
DR Proteomes; UP000299011; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
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 Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR InterPro; IPR045031; DHP_synth-like.
DR InterPro; IPR006390; DHP_synth_dom.
DR InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR InterPro; IPR001645; Folylpolyglutamate_synth.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR004101; Mur_ligase_C.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR InterPro; IPR000489; Pterin-binding_dom.
DR NCBIfam; TIGR01496; DHPS; 1.
DR NCBIfam; TIGR01499; folC; 1.
DR PANTHER; PTHR20941; FOLATE SYNTHESIS PROTEINS; 1.
DR PANTHER; PTHR20941:SF1; FOLIC ACID SYNTHESIS PROTEIN FOL1; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR Pfam; PF00809; Pterin_bind; 1.
DR SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 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:QCQ75302.1}.
FT DOMAIN 552..802
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 816 AA; 87964 MW; C8B06E27CBC5D98D CRC64;
MEYHEAVNFL FDLRRFQVKP GTESIQRLLS HLGDPHEGVS FVQVAGSNGK GSTARMLDST
LREAGQSVGL YTSPHFDNVR ERVRVDGRKI PESALSAFVA EAKPYLVERA ADGEPLTFFE
TVTALAIWYF DQADVDVAVL EVGMGGELDA TSAVDPVASA VTNVSLEHTA VLGDTIEEIA
RTKAAVAPAD NPLVTGAAGD ALDVIREEVG DVLTVGGADA DTDVRTAYGG RVNHQEAAVT
VETDDETLDL RIPLLGAYQA RNAGIAVALS RQVRPDISDD EIHRGLRNAH WPGRFEVMGT
DPMVVLDGAH NPDACAQVAT VLDEFEYDDL HLVYGAMHDK DHGEMVEALP DVASVVTCHA
DISRAEDPEI LASVFERIDV PEVETGDVVA SALERARERA DPDDCVLVVG SLYVVAEART
TWTRAIIPKT HRTLDDARET LERANVADEG SRDERAAKAV HQTVHTRVQR RQARHLREEL
FSIGGDCAVS GHESGGELVD VVLMGTLDQF DRLTENLRDR PYALPELADE IEASLGRDPS
AETHGYPWED GPSVMGILNV TPDSFHDGGE FYDIEDAVEQ AEAMVEAGVG IIDVGGESTR
PGAEEVPVDE EIRRVTPVIE ALSDLDALVS VDTRKAAVAE AALDAGADIL NDVTGLEDPE
MRFLAAERDV PVIVMHSIDA PVIPDKDIDY DDVVEDVIDE LTERVLLAEK AGIPRRNIIV
DPGLGFGKSK AENFELLGRV DEFRALGCPV LIGHSHKSMF SLVGEKTGDN LAATIAGTAI
AADRGADIIR VHDVPENVAA VNVALASQDS SRFTDE
//
