FOLB2_ARATH
ID FOLB2_ARATH Reviewed; 131 AA.
AC Q9FM54;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Dihydroneopterin aldolase 2 {ECO:0000305};
DE Short=DHNA2 {ECO:0000305};
DE EC=4.1.2.25 {ECO:0000269|PubMed:15107504};
DE AltName: Full=7,8-dihydroneopterin aldolase;
DE AltName: Full=AtFolB2 {ECO:0000303|PubMed:15107504};
GN Name=FOLB2 {ECO:0000303|PubMed:15107504};
GN OrderedLocusNames=At5g62980 {ECO:0000312|Araport:AT5G62980};
GN ORFNames=MJH22.3 {ECO:0000312|EMBL:BAB08841.1};
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND 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:0000269|PubMed:15107504}.
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:0000269|PubMed:15107504};
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 -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and siliques.
CC {ECO:0000269|PubMed:15107504}.
CC -!- SIMILARITY: Belongs to the DHNA family. {ECO:0000305}.
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DR EMBL; AB009051; BAB08841.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97682.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70563.1; -; Genomic_DNA.
DR EMBL; BT003970; AAO42014.1; -; mRNA.
DR EMBL; BT014860; AAT41843.1; -; mRNA.
DR RefSeq; NP_001332160.1; NM_001345573.1.
DR RefSeq; NP_201103.1; NM_125692.4.
DR AlphaFoldDB; Q9FM54; -.
DR SMR; Q9FM54; -.
DR STRING; 3702.AT5G62980.1; -.
DR PaxDb; Q9FM54; -.
DR PRIDE; Q9FM54; -.
DR ProteomicsDB; 228915; -.
DR EnsemblPlants; AT5G62980.1; AT5G62980.1; AT5G62980.
DR EnsemblPlants; AT5G62980.2; AT5G62980.2; AT5G62980.
DR GeneID; 836418; -.
DR Gramene; AT5G62980.1; AT5G62980.1; AT5G62980.
DR Gramene; AT5G62980.2; AT5G62980.2; AT5G62980.
DR KEGG; ath:AT5G62980; -.
DR Araport; AT5G62980; -.
DR TAIR; locus:2166300; AT5G62980.
DR eggNOG; ENOG502RZV8; Eukaryota.
DR HOGENOM; CLU_112632_1_0_1; -.
DR InParanoid; Q9FM54; -.
DR OMA; GTSENDM; -.
DR OrthoDB; 1383549at2759; -.
DR PhylomeDB; Q9FM54; -.
DR BioCyc; ARA:AT5G62980-MON; -.
DR BRENDA; 4.1.2.25; 399.
DR BRENDA; 5.1.99.8; 399.
DR UniPathway; UPA00077; UER00154.
DR PRO; PR:Q9FM54; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FM54; baseline and differential.
DR Genevisible; Q9FM54; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004150; F:dihydroneopterin aldolase activity; IDA:TAIR.
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 1: Evidence at protein level;
KW Folate biosynthesis; Lyase; Reference proteome.
FT CHAIN 1..131
FT /note="Dihydroneopterin aldolase 2"
FT /id="PRO_0000431446"
FT ACT_SITE 107
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9SF23"
FT BINDING 29
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AC16"
FT BINDING 61
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AC16"
FT BINDING 80..81
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AC16"
SQ SEQUENCE 131 AA; 14685 MW; 194C4731D1554D48 CRC64;
MEKDMAMMGD KLILRGLKFY GFHGAIPEEK TLGQMFMLDI DAWMCLKKAG LSDNLADSVS
YVDIYNVAKE VVEGSSRNLL ERVAGLIASK TLEISPRITA VRVKLWKPNV ALIQSTIDYL
GVEIFRDRAT E
