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Database: UniProt
Entry: D2S293_HALTV
LinkDB: D2S293_HALTV
Original site: D2S293_HALTV 
ID   D2S293_HALTV            Unreviewed;       810 AA.
AC   D2S293;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458};
DE            EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458};
GN   OrderedLocusNames=Htur_4713 {ECO:0000313|EMBL:ADB63490.1};
OS   Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS   13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OG   Plasmid pHTUR02 {ECO:0000313|EMBL:ADB63490.1,
OG   ECO:0000313|Proteomes:UP000001903}.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Haloterrigena.
OX   NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB63490.1, ECO:0000313|Proteomes:UP000001903};
RN   [1] {ECO:0000313|EMBL:ADB63490.1, ECO:0000313|Proteomes:UP000001903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 /
RC   4k {ECO:0000313|Proteomes:UP000001903};
RC   PLASMID=pHTUR02 {ECO:0000313|EMBL:ADB63490.1,
RC   ECO:0000313|Proteomes:UP000001903};
RX   PubMed=21304683; DOI=10.4056/sigs.681272;
RA   Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A.,
RA   Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA   Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Haloterrigena turkmenica type strain (4k).";
RL   Stand. Genomic Sci. 2:107-116(2010).
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; CP001862; ADB63490.1; -; Genomic_DNA.
DR   RefSeq; WP_012945734.1; NC_013745.1.
DR   AlphaFoldDB; D2S293; -.
DR   GeneID; 8745308; -.
DR   KEGG; htu:Htur_4713; -.
DR   HOGENOM; CLU_017222_0_0_2; -.
DR   OrthoDB; 75177at2157; -.
DR   Proteomes; UP000001903; Plasmid pHTUR02.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004156; F:dihydropteroate synthase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
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.
DR   InterPro; IPR006390; DHP_synth_dom.
DR   InterPro; IPR011005; Dihydropteroate_synth-like.
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   Plasmid {ECO:0000313|EMBL:ADB63490.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          549..801
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50972"
SQ   SEQUENCE   810 AA;  87353 MW;  4422D3FD7A2CD3BA CRC64;
     MEYHESVDYL ESLQRRRPKL GTETTAALLT HLDRPHEDLD CVQIAGSNGK GSTACMLERV
     LRDAGLDVGL YTSPDLNDLR ERIQINGRKI PKQRVQEFVA EIDDCVERLR EVDDTPTYFE
     VLTALALHHF ANEDVDVAVL EVGIGGRYDA TSAVDPVASA VTSVSLEHTD ILGDTIEEIA
     RDKAQVSPAD APLVTGASGA ALEAIRSETD VITVGSDDAD VVAREHGLAS PIESEISIAG
     PKWSFETRLP LVGPHQATNA GVAATLADQV AGVDPESIAR GLRDSYWPGR FEVMSTTPLA
     ILDGAHNPGA CETLASLVDR YSFDDLHLVF GAMREKDHRG MAAALPSPDA LYLCEPDVPR
     AENTDALAAA FDDRPATIDC AGSVLEATER ALSAADEGDC VLVTGSLYAV AEARDRWTRL
     QIPKRTAATE QARNVLTSAA VDAETAESVA DETVHRTIKT YLRGPQAERV EQAFEAIGGT
     CVRSDAETAG RRVVTILSGT SSQFRDLFEE LTDADRGLAH VAAQLRRTID DDRVDERADR
     DRYPWDRTPA VMGILNVTPD SFYDGGEYDR VPDAVRQARE MVAAGADIID VGGESTRPGA
     EPVSVAEEID RVVPVIERIA DLDPDVPISV DTRKAAVADA ALEAGADIVN DVSGLEDPEM
     RFVVADHDAS LVIMHSLETP VNPDRTVTYD DVVEDVLHEL SETVLLAERA GLDRDQIVVD
     PGLGFGKNPA ESFELAARID ELRALGCPIM IGHSRKSMFD RVGCEPGERL PPTLAVTTMA
     AERGADVVRV HDVSENAAAV RTVRTADARY
//
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