ID D9T0V6_MICAI Unreviewed; 613 AA.
AC D9T0V6;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458};
DE EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458};
GN OrderedLocusNames=Micau_1778 {ECO:0000313|EMBL:ADL45331.1};
OS Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / BCRC 12538 / CBS
OS 129.76 / JCM 10878 / NBRC 16125 / NRRL B-16091 / INA 9442).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=644283 {ECO:0000313|EMBL:ADL45331.1, ECO:0000313|Proteomes:UP000001908};
RN [1] {ECO:0000313|EMBL:ADL45331.1, ECO:0000313|Proteomes:UP000001908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442
RC {ECO:0000313|Proteomes:UP000001908};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Hirsch A.M., Woyke T.;
RT "Complete sequence of Micromonospora aurantiaca ATCC 27029.";
RL Submitted (AUG-2010) 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; CP002162; ADL45331.1; -; Genomic_DNA.
DR AlphaFoldDB; D9T0V6; -.
DR STRING; 644283.Micau_1778; -.
DR KEGG; mau:Micau_1778; -.
DR eggNOG; COG0294; Bacteria.
DR eggNOG; COG5014; Bacteria.
DR HOGENOM; CLU_445369_0_0_11; -.
DR OrthoDB; 9782387at2; -.
DR Proteomes; UP000001908; Chromosome.
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 CDD; cd00739; DHPS; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1.
DR InterPro; IPR013785; Aldolase_TIM.
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 SUPFAM; SSF102114; Radical SAM enzymes; 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:UP000001908};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADL45331.1}.
FT DOMAIN 13..272
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 613 AA; 67209 MW; E616327A4355F8CF CRC64;
MRSTLLQPRH GVPFVLGLLN MTPGSFSDGG FYLRHEGAIV HAEAIWQQGA EVIDVGGEST
RPGAGRTDAD TETQRVRPVL RTLTELGIPT SIDTTRATVV AAALDVGAAL VSDVSVGLAD
RNMASVVLDS GCPWVLTHRR GHSRWMSQLA EDGDAVIEVR AELRPRVNAA VSAGVAPDKL
IVDPGIGFAK TTEHIWRLSA CIGAVLDLGL PVLFGSSRKS YLGTLLAGAG GIPRPADERN
AATLATTVLA VLQGVWGRYG PITCSPTVDA LAVLRAHGGA SMMNPHDSAP GRTGMRQRVV
RPERQEFLIA RLDRSLESKD AYTRVNCGGF GRVRRFNTFA IHLRARESRL PVRAHFRGLP
RVLPYHTQVF QLAGCNWNCW YCFVDDELLV GDASRGAFLT ATQIIDLYMA EPDPPPVLDL
SGGQPDLVPE WCLWIMRELE RRGLRGSVFV WVDDNLSGRF MRQYLSRPDI AYMASFPNHS
RVGCFKGFNE SSFVFNTKAA PGGFSRQFDV FKDLITDGFD MYAYATFTSP DMTGVDRAMG
EFVDRLQEVH PNLPLRTIPL EVRRYSAVGG RGVGPIEPLL ARQDIAAQAW ERELTSRYTS
AELATPYEDV DLT
//
