FOLB3_ARATH
ID FOLB3_ARATH Reviewed; 160 AA.
AC Q6GKX5; Q9LSZ1;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Probable dihydroneopterin aldolase 3 {ECO:0000305};
DE Short=DHNA3 {ECO:0000305};
DE EC=4.1.2.25 {ECO:0000269|PubMed:15107504};
DE AltName: Full=7,8-dihydroneopterin aldolase;
DE AltName: Full=AtFolB3 {ECO:0000303|PubMed:15107504};
GN Name=FOLB3 {ECO:0000303|PubMed:15107504};
GN OrderedLocusNames=At3g21730 {ECO:0000312|Araport:AT3G21730};
GN ORFNames=MSD21.4 {ECO:0000312|EMBL:BAB02835.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=15107504; DOI=10.1104/pp.103.038430;
RA Goyer A., Illarionova V., Roje S., Fischer M., Bacher A., Hanson A.D.;
RT "Folate biosynthesis in higher plants. cDNA cloning, heterologous
RT expression, and characterization of dihydroneopterin aldolases.";
RL Plant Physiol. 135:103-111(2004).
CC -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin into 6-
CC hydroxymethyl-7,8-dihydropterin, a biosynthetic precursor of the
CC vitamin tetrahydrofolate. Can use L-threo-dihydroneopterin and D-
CC erythro-dihydroneopterin as substrates for the formation of 6-
CC hydroxymethyldihydropterin, but it can also catalyze the epimerization
CC of carbon 2' of dihydroneopterin and dihydromonapterin.
CC {ECO:0000250|UniProtKB:Q9SF23}.
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 Evidence={ECO:0000250|UniProtKB:Q9SF23};
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. {ECO:0000305}.
CC -!- SUBUNIT: Homooctamer. Forms a hollow cylinder assembled from two ring-
CC shaped tetramers. {ECO:0000250|UniProtKB:Q9SF23}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q6GKX5-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed at very low levels in siliques.
CC {ECO:0000269|PubMed:15107504}.
CC -!- SIMILARITY: Belongs to the DHNA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02835.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB025634; BAB02835.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76545.1; -; Genomic_DNA.
DR EMBL; BT014939; AAT47790.1; -; mRNA.
DR EMBL; BT015391; AAU05514.1; -; mRNA.
DR RefSeq; NP_188810.2; NM_113068.3. [Q6GKX5-1]
DR AlphaFoldDB; Q6GKX5; -.
DR SMR; Q6GKX5; -.
DR STRING; 3702.AT3G21730.1; -.
DR iPTMnet; Q6GKX5; -.
DR PaxDb; Q6GKX5; -.
DR PRIDE; Q6GKX5; -.
DR ProteomicsDB; 228941; -. [Q6GKX5-1]
DR EnsemblPlants; AT3G21730.1; AT3G21730.1; AT3G21730. [Q6GKX5-1]
DR GeneID; 821727; -.
DR Gramene; AT3G21730.1; AT3G21730.1; AT3G21730. [Q6GKX5-1]
DR KEGG; ath:AT3G21730; -.
DR Araport; AT3G21730; -.
DR TAIR; locus:2093054; AT3G21730.
DR eggNOG; ENOG502RZV8; Eukaryota.
DR InParanoid; Q6GKX5; -.
DR OMA; CNSANKR; -.
DR PhylomeDB; Q6GKX5; -.
DR BioCyc; ARA:AT3G21730-MON; -.
DR UniPathway; UPA00077; UER00154.
DR PRO; PR:Q6GKX5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q6GKX5; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004150; F:dihydroneopterin aldolase activity; IBA:GO_Central.
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 PANTHER; PTHR42844; PTHR42844; 1.
DR Pfam; PF02152; FolB; 1.
DR SMART; SM00905; FolB; 1.
DR TIGRFAMs; TIGR00525; folB; 1.
DR TIGRFAMs; TIGR00526; folB_dom; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Folate biosynthesis; Lyase; Reference proteome.
FT CHAIN 1..160
FT /note="Probable dihydroneopterin aldolase 3"
FT /id="PRO_0000431447"
FT ACT_SITE 137
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9SF23"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AC16"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AC16"
FT BINDING 110..111
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AC16"
SQ SEQUENCE 160 AA; 18035 MW; 2853FD8087D521F9 CRC64;
MHSSLKTMAP AKLERLCVLS FFLFCATVFG TESLESLPED KLILRGLKFY GFHGVLPEER
ELGGLFIVDI NLWLSLKKAI ESDNLADTVS FADTFRLVKK IVEGPPRNLY ETVADDIASE
MLETFPKINV IRVKFGKPNP SLVNSTVDFL GAELFRKRNH
