ID D0L432_GORB4 Unreviewed; 283 AA.
AC D0L432;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458};
DE EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458};
GN OrderedLocusNames=Gbro_4015 {ECO:0000313|EMBL:ACY23185.1};
OS Gordonia bronchialis (strain ATCC 25592 / DSM 43247 / BCRC 13721 / JCM 3198
OS / KCTC 3076 / NBRC 16047 / NCTC 10667) (Rhodococcus bronchialis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=526226 {ECO:0000313|EMBL:ACY23185.1, ECO:0000313|Proteomes:UP000001219};
RN [1] {ECO:0000313|Proteomes:UP000001219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25592 / DSM 43247 / BCRC 13721 / JCM 3198 / KCTC 3076 /
RC NBRC 16047 / NCTC 10667 {ECO:0000313|Proteomes:UP000001219};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Ovchinnikova G., Saunders E., Brettin T., Detter J.C., Han C., Larimer F.,
RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA Wu D., Jando M., Schneider S., Goeker M., Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of Gordonia bronchialis DSM 43247.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACY23185.1, ECO:0000313|Proteomes:UP000001219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25592 / DSM 43247 / BCRC 13721 / JCM 3198 / KCTC 3076 /
RC NBRC 16047 / NCTC 10667 {ECO:0000313|Proteomes:UP000001219};
RX PubMed=21304674;
RA Ivanova N., Sikorski J., Jando M., Lapidus A., Nolan M., Lucas S.,
RA Del Rio T.G., Tice H., Copeland A., Cheng J.F., Chen F., Bruce D.,
RA Goodwin L., Pitluck S., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA Saunders E., Han C., Detter J.C., Brettin T., Rohde M., Goker M.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA Kyrpides N.C.;
RT "Complete genome sequence of Gordonia bronchialis type strain (3410).";
RL Stand. Genomic Sci. 2:19-28(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; CP001802; ACY23185.1; -; Genomic_DNA.
DR RefSeq; WP_012835688.1; NC_013441.1.
DR AlphaFoldDB; D0L432; -.
DR STRING; 526226.Gbro_4015; -.
DR KEGG; gbr:Gbro_4015; -.
DR eggNOG; COG0294; Bacteria.
DR HOGENOM; CLU_008023_0_1_11; -.
DR OrthoDB; 9811744at2; -.
DR Proteomes; UP000001219; 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; 3.20.20.20; 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; 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:UP000001219};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACY23185.1}.
FT DOMAIN 1..264
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 283 AA; 28833 MW; 19271383922FD085 CRC64;
MGVINVTADS FSDGGRYLDT AAAVEHGLAL RAEGADLIDV GGESTRPGAI RVDPDLEAAR
VTPVISALSG HGARISVDTM RASVAAAAID AGATVVNDVS GGRADADMAK VVADAGLPWI
LMHWRPAGDS TDRHFTHRIG DVGGYRDVVA EVSGELLAQV DAAVSAGVDP DHIILDPGLG
FAKTAEHNWA LLHALPTLVG LGFPVLVGAS RKRFLGTLLA GDDGTVRPPQ ERDVATASIS
ALAAMNGAWG VRVHDVAASR DAVAVAAAWR AGGSRSTPDG AHG
//
