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Database: UniProt
Entry: A0A0G3HB79_9CORY
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ID   A0A0G3HB79_9CORY        Unreviewed;       277 AA.
AC   A0A0G3HB79;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Dihydropteroate synthase {ECO:0000256|RuleBase:RU361205};
DE            Short=DHPS {ECO:0000256|RuleBase:RU361205};
DE            EC=2.5.1.15 {ECO:0000256|RuleBase:RU361205};
DE   AltName: Full=Dihydropteroate pyrophosphorylase {ECO:0000256|RuleBase:RU361205};
GN   Name=folP2 {ECO:0000313|EMBL:AKK08422.1};
GN   ORFNames=CTEST_04875 {ECO:0000313|EMBL:AKK08422.1};
OS   Corynebacterium testudinoris.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=136857 {ECO:0000313|EMBL:AKK08422.1, ECO:0000313|Proteomes:UP000035540};
RN   [1] {ECO:0000313|EMBL:AKK08422.1, ECO:0000313|Proteomes:UP000035540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44614 {ECO:0000313|EMBL:AKK08422.1,
RC   ECO:0000313|Proteomes:UP000035540};
RX   PubMed=26227591;
RA   Ruckert C., Kriete M., Jaenicke S., Winkler A., Tauch A.;
RT   "Complete Genome Sequence of the Type Strain Corynebacterium testudinoris
RT   DSM 44614, Recovered from Necrotic Lesions in the Mouth of a Tortoise.";
RL   Genome Announc. 3:e00784-15(2015).
RN   [2] {ECO:0000313|Proteomes:UP000035540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44614 {ECO:0000313|Proteomes:UP000035540};
RA   Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT   "Complete genome sequence of Corynebacterium testudinoris DSM 44614,
RT   recovered from necrotic lesions in the mouth of a tortoise.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with
CC       6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-
CC       dihydropteroate (H2Pte), the immediate precursor of folate derivatives.
CC       {ECO:0000256|RuleBase:RU361205}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU361205};
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|RuleBase:RU361205}.
CC   -!- SIMILARITY: Belongs to the DHPS family.
CC       {ECO:0000256|RuleBase:RU361205}.
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DR   EMBL; CP011545; AKK08422.1; -; Genomic_DNA.
DR   RefSeq; WP_047252784.1; NZ_CP011545.1.
DR   AlphaFoldDB; A0A0G3HB79; -.
DR   STRING; 136857.CTEST_04875; -.
DR   KEGG; cted:CTEST_04875; -.
DR   PATRIC; fig|136857.5.peg.969; -.
DR   OrthoDB; 9811744at2; -.
DR   UniPathway; UPA00077; UER00156.
DR   Proteomes; UP000035540; 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   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00739; DHPS; 1.
DR   Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1.
DR   InterPro; IPR045031; DHP_synth.
DR   InterPro; IPR006390; DHP_synth_dom.
DR   InterPro; IPR011005; Dihydropteroate_synth-like.
DR   InterPro; IPR000489; Pterin-binding_dom.
DR   NCBIfam; TIGR01496; DHPS; 1.
DR   PANTHER; PTHR20941; FOLATE SYNTHESIS PROTEINS; 1.
DR   PANTHER; PTHR20941:SF8; INACTIVE DIHYDROPTEROATE SYNTHASE 2; 1.
DR   Pfam; PF00809; Pterin_bind; 1.
DR   SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR   PROSITE; PS00792; DHPS_1; 1.
DR   PROSITE; PS00793; DHPS_2; 1.
DR   PROSITE; PS50972; PTERIN_BINDING; 1.
PE   3: Inferred from homology;
KW   Folate biosynthesis {ECO:0000256|RuleBase:RU361205};
KW   Magnesium {ECO:0000256|RuleBase:RU361205};
KW   Metal-binding {ECO:0000256|RuleBase:RU361205};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035540};
KW   Transferase {ECO:0000256|RuleBase:RU361205, ECO:0000313|EMBL:AKK08422.1}.
FT   DOMAIN          5..258
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50972"
SQ   SEQUENCE   277 AA;  29517 MW;  D1DB22B76D5DC4CD CRC64;
     MNQLPAIMAI VNRTPDSFYD QGATFADQAA LDRCAQVIDE GASIVDIGGV KAGPGAEVSA
     SEEMDRIVPT IAAVAKQHPD IVISVDTWRA EVADAAIRAG ATLVNDTWAG HDPELVEVAG
     QHRVGYVCSH TGGVVPRTRP HRVHFDDVVA DVIAETTRLA EKAVACGVPE DKIYLDPTHD
     FGKNTFHGLE LLRRIDELVA TGWPVLMALS NKDFVGETLD RPVGERVAGT LAATAWAAAR
     GVAAFRVHEV AETLDVVRMT AAIQGTFPPM NTVRGLA
//
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