ID C7MM10_CRYCD Unreviewed; 436 AA.
AC C7MM10;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Dihydropteroate synthase/2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase {ECO:0000313|EMBL:ACU93950.1};
GN OrderedLocusNames=Ccur_02190 {ECO:0000313|EMBL:ACU93950.1};
OS Cryptobacterium curtum (strain ATCC 700683 / DSM 15641 / CCUG 43107 /
OS 12-3).
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Cryptobacterium.
OX NCBI_TaxID=469378 {ECO:0000313|EMBL:ACU93950.1, ECO:0000313|Proteomes:UP000000954};
RN [1] {ECO:0000313|EMBL:ACU93950.1, ECO:0000313|Proteomes:UP000000954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700683 / DSM 15641 / 12-3
RC {ECO:0000313|Proteomes:UP000000954};
RX PubMed=21304644; DOI=10.40456/sigs.12260;
RA Mavrommatis K., Pukall R., Rohde C., Chen F., Sims D., Brettin T.,
RA Kuske C., Detter J.C., Han C., Lapidus A., Copeland A., Glavina Del Rio T.,
RA Nolan M., Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA Ovchinnikova G., Pati A., Ivanova N., Chen A., Palaniappan K., Chain P.,
RA D'haeseleer P., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Rohde M., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Cryptobacterium curtum type strain (12-3).";
RL Stand. Genomic Sci. 1:93-100(2009).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-
CC 6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841,
CC ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000198};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-
CC 4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-
CC dihydroneopterin triphosphate: step 4/4.
CC {ECO:0000256|ARBA:ARBA00005051}.
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}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the DHPS family.
CC {ECO:0000256|ARBA:ARBA00009951}.
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DR EMBL; CP001682; ACU93950.1; -; Genomic_DNA.
DR RefSeq; WP_012802639.1; NC_013170.1.
DR AlphaFoldDB; C7MM10; -.
DR STRING; 469378.Ccur_02190; -.
DR KEGG; ccu:Ccur_02190; -.
DR eggNOG; COG0294; Bacteria.
DR eggNOG; COG0801; Bacteria.
DR HOGENOM; CLU_032711_0_0_11; -.
DR OrthoDB; 9811744at2; -.
DR UniPathway; UPA00077; UER00155.
DR Proteomes; UP000000954; Chromosome.
DR GO; GO:0003848; F:2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004156; F:dihydropteroate synthase activity; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00739; DHPS; 1.
DR CDD; cd00483; HPPK; 1.
DR Gene3D; 3.30.70.560; 7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK; 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; IPR000550; Hppk.
DR InterPro; IPR035907; Hppk_sf.
DR InterPro; IPR000489; Pterin-binding_dom.
DR NCBIfam; TIGR01496; DHPS; 1.
DR NCBIfam; TIGR01498; folK; 1.
DR PANTHER; PTHR20941; FOLATE SYNTHESIS PROTEINS; 1.
DR PANTHER; PTHR20941:SF1; FOLIC ACID SYNTHESIS PROTEIN FOL1; 1.
DR Pfam; PF01288; HPPK; 1.
DR Pfam; PF00809; Pterin_bind; 1.
DR SUPFAM; SSF55083; 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK; 1.
DR SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR PROSITE; PS00792; DHPS_1; 1.
DR PROSITE; PS00793; DHPS_2; 1.
DR PROSITE; PS00794; HPPK; 1.
DR PROSITE; PS50972; PTERIN_BINDING; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ACU93950.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000954};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 15..267
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 436 AA; 47347 MW; B2AEA1CB7F8AA3DE CRC64;
MIWKCGNYSF DTQVPVVMGI LNVTPDSFSD GGSYASFDDA IAAACRMRDE GALIIDVGGE
STRPGAAEVS EDEELHRVLD VVRALAANDI CVSIDTRHAS VAAACVDAGA SIINDVSGFR
DPEMVRVAAS CDAGLVVMHM RGEPRTMQQE PQYDDVVVEV RDYLLAQAHM LESAGVDRAR
ICIDPGPGFG KTAQQTVELV RNIQEFVRTG YPVMIAVSRK SYIGALYSIE VPQDRDKASA
EEALMACELG ACVVRTHNVA ATVARLADVR PYAFIGLGCN VALVGSAEES QQSKIAQLEH
AIAEICLIPD TQLIDVSGFY ESEPAYLEDQ DTFVNAVALI RTGITPRDLL HYLQAIEDSL
GRVRTVKNGP RTCDLDILDY QLYLSSDEEL TVPHPLLAER DFVVKPLLEL APFHILANGK
RLTADAVKVG HAVRIR
//
