FOLB_CHLMU
ID FOLB_CHLMU Reviewed; 122 AA.
AC Q9PJC6;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Probable dihydroneopterin aldolase;
DE Short=DHNA;
DE EC=4.1.2.25;
DE AltName: Full=7,8-dihydroneopterin aldolase;
GN Name=folB; OrderedLocusNames=TC_0904;
OS Chlamydia muridarum (strain MoPn / Nigg).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=243161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MoPn / Nigg;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
CC -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-
CC hydroxymethyl-7,8-dihydropterin. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin +
CC glycolaldehyde; Xref=Rhea:RHEA:10540, ChEBI:CHEBI:17001,
CC ChEBI:CHEBI:17071, ChEBI:CHEBI:44841; EC=4.1.2.25;
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-
CC 4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-
CC dihydroneopterin triphosphate: step 3/4.
CC -!- SIMILARITY: Belongs to the DHNA family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE002160; AAF39697.1; -; Genomic_DNA.
DR PIR; H81652; H81652.
DR RefSeq; WP_010231896.1; NZ_CP027217.1.
DR AlphaFoldDB; Q9PJC6; -.
DR SMR; Q9PJC6; -.
DR STRING; 243161.TC_0904; -.
DR EnsemblBacteria; AAF39697; AAF39697; TC_0904.
DR GeneID; 1246273; -.
DR KEGG; cmu:TC_0904; -.
DR eggNOG; COG1539; Bacteria.
DR HOGENOM; CLU_112632_3_0_0; -.
DR OMA; QIGSACF; -.
DR OrthoDB; 1858654at2; -.
DR UniPathway; UPA00077; UER00154.
DR Proteomes; UP000000800; Chromosome.
DR GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:UniProtKB-EC.
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; cd00534; DHNA_DHNTPE; 1.
DR Gene3D; 3.30.1130.10; -; 1.
DR InterPro; IPR006156; Dihydroneopterin_aldolase.
DR InterPro; IPR006157; FolB_dom.
DR InterPro; IPR043133; GTP-CH-I_C/QueF.
DR Pfam; PF02152; FolB; 1.
DR SMART; SM00905; FolB; 1.
DR TIGRFAMs; TIGR00525; folB; 1.
DR TIGRFAMs; TIGR00526; folB_dom; 1.
PE 3: Inferred from homology;
KW Folate biosynthesis; Lyase.
FT CHAIN 1..122
FT /note="Probable dihydroneopterin aldolase"
FT /id="PRO_0000168266"
FT ACT_SITE 101
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AC16"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AC16"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AC16"
FT BINDING 73..74
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AC16"
SQ SEQUENCE 122 AA; 13770 MW; 3105FF86D2420A47 CRC64;
MYRLDVTNFR VWVSIGVSEQ ERYHKQPILV SVSLVFREEP KVCSTDEISD GICYAALVSL
IEQTAANHPC ALLERLAKVL LEKLEESLAQ FVCKIDLRVS KERPPIPNLL SPVSFSISKE
VP
