ID Q5V5Y3_HALMA Unreviewed; 799 AA.
AC Q5V5Y3;
DT 07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 07-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458};
DE EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458};
GN Name=folP2 {ECO:0000313|EMBL:AAV45069.1};
GN Synonyms=folP {ECO:0000313|EMBL:QCP90031.1};
GN OrderedLocusNames=pNG7379 {ECO:0000313|EMBL:AAV45069.1};
GN ORFNames=E6P14_03900 {ECO:0000313|EMBL:QCP90031.1};
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OG Plasmid pHMA411 {ECO:0000313|EMBL:QCP90031.1},
OG Plasmid pNG700 {ECO:0000313|EMBL:AAV45069.1,
OG ECO:0000313|Proteomes:UP000001169}, and
OG Plasmid phma411 {ECO:0000313|Proteomes:UP000298722}.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569 {ECO:0000313|EMBL:AAV45069.1, ECO:0000313|Proteomes:UP000001169};
RN [1] {ECO:0000313|EMBL:AAV45069.1, ECO:0000313|Proteomes:UP000001169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 {ECO:0000313|EMBL:AAV45069.1}, and ATCC 43049 / DSM
RC 3752 / JCM 8966 / VKM B-1809 {ECO:0000313|Proteomes:UP000001169};
RC PLASMID=Plasmid pNG700 {ECO:0000313|Proteomes:UP000001169}, and pNG700
RC {ECO:0000313|EMBL:AAV45069.1};
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
RN [2] {ECO:0000313|EMBL:QCP90031.1, ECO:0000313|Proteomes:UP000298722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 {ECO:0000313|EMBL:QCP90031.1,
RC ECO:0000313|Proteomes:UP000298722};
RC PLASMID=pHMA411 {ECO:0000313|EMBL:QCP90031.1}, and phma411
RC {ECO:0000313|Proteomes:UP000298722};
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}.
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DR EMBL; AY596296; AAV45069.1; -; Genomic_DNA.
DR EMBL; CP039137; QCP90031.1; -; Genomic_DNA.
DR RefSeq; WP_011222755.1; NZ_CP039137.1.
DR AlphaFoldDB; Q5V5Y3; -.
DR EnsemblBacteria; AAV45069; AAV45069; pNG7379.
DR GeneID; 40151269; -.
DR KEGG; hma:pNG7379; -.
DR PATRIC; fig|272569.17.peg.799; -.
DR HOGENOM; CLU_017222_0_0_2; -.
DR Proteomes; UP000001169; Plasmid pNG700.
DR Proteomes; UP000298722; Plasmid phma411.
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 Plasmid {ECO:0000313|EMBL:AAV45069.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001169};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AAV45069.1}.
FT DOMAIN 534..784
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 799 AA; 85133 MW; 871CD80EC1FBA5AF CRC64;
MEYHESADYL QSLQRRRPKL GTDTTARMLS HLGDPDGSFD SVQIAGSNGK GSTARMTESV
LRAAGLDVGL FTSPGLNGFR EQITVNGGRV PKARVTEFVE QIEPCINQLA AEDDKPTHFE
VLTALALYHF DVEDVDVAVL EVGIGGRYDA TSAVDPVASA VTSISLEHTD LLGDTIEEIA
RDKGQVAPSD APLVTGTAGA ALDAIQEITD TITVGSEAAD VTATENGMRS AVENRISLTG
SNWALESNLK LLGQHQAENA GVAATLARQL IDVDTETISE GLRAATLPGR FEVRSTDPMV
VLDGSHNPGA METLTTLIGR YEYDDLHVVF AAMQDKEYEQ MIATLPAVET AFATRPAVDR
AASTESLAAA FEGQAAQIQQ VESVPEATER AIATAGEDDF VLVAGSLYAV AEARDRWSRL
VVPKENLQQA STGETAGVEN EPQLHQQMLS VTLRRDQAGV VKQEFEDCGG TCTCSTVGMP
EKLVDTTLSG TPRQFQQLTD RLASAGLGLG CLAIQFEEML SERSFPPPFD GEEAAVMGIL
NVTPDSFYDG GEYNRRDLAI SHAEQMIESG ADIVDIGGES TRPGAEPVSI ETEIDRVVPV
IEAVSSLDTT VSVDTRKAAV ADAALDAGAD IVNDVSGLSD PEMRFVVADH DASVILMHSL
SAPVDPGRTV TYDDVVDDVL RDLTEQILLA EQAGIDREQI IIDPGCGFGK NAAESFELVD
RLHEFQALGC PVLVGHSRKS MFAEMSDAEA DRLPPTLATT ALAAERGADA VRVHDVSENN
AVLKTVSATA ARPSQLRQQ
//
