FOLB1_ARATH
ID FOLB1_ARATH Reviewed; 146 AA.
AC Q9SF23; A2RVT4; Q6R8J1;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Dihydroneopterin aldolase 1 {ECO:0000305};
DE Short=DHNA1 {ECO:0000305};
DE EC=4.1.2.25 {ECO:0000269|PubMed:15107504, ECO:0000269|PubMed:15165863};
DE AltName: Full=7,8-dihydroneopterin aldolase;
DE AltName: Full=AtFolB1 {ECO:0000303|PubMed:15107504};
GN Name=FOLB1 {ECO:0000303|PubMed:15107504}; OrderedLocusNames=At3g11750;
GN ORFNames=F26K24.4;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
RA Kim C.J., Bautista V.R., Chen H., De Los Reyes C., Wu S.Y., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-146, PROTEIN SEQUENCE OF 22-31, X-RAY
RP CRYSTALLOGRAPHY (2.2 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE,
RP AND SUBUNIT.
RX PubMed=15165863; DOI=10.1016/j.jmb.2004.04.034;
RA Bauer S., Schott A.K., Illarionova V., Bacher A., Huber R., Fischer M.;
RT "Biosynthesis of tetrahydrofolate in plants: crystal structure of 7,8-
RT dihydroneopterin aldolase from Arabidopsis thaliana reveals a novel adolase
RT class.";
RL J. Mol. Biol. 339:967-979(2004).
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, ECO:0000269|PubMed:15165863}.
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, ECO:0000269|PubMed:15165863};
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:0000269|PubMed:15165863}.
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; AC016795; AAF23191.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75093.1; -; Genomic_DNA.
DR EMBL; BT030075; ABN04813.1; -; mRNA.
DR EMBL; AY507667; AAR88082.1; -; mRNA.
DR RefSeq; NP_187781.1; NM_112008.2.
DR PDB; 1SQL; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-146.
DR PDBsum; 1SQL; -.
DR AlphaFoldDB; Q9SF23; -.
DR SMR; Q9SF23; -.
DR BioGRID; 5682; 1.
DR STRING; 3702.AT3G11750.1; -.
DR iPTMnet; Q9SF23; -.
DR PaxDb; Q9SF23; -.
DR PRIDE; Q9SF23; -.
DR ProteomicsDB; 247375; -.
DR EnsemblPlants; AT3G11750.1; AT3G11750.1; AT3G11750.
DR GeneID; 820348; -.
DR Gramene; AT3G11750.1; AT3G11750.1; AT3G11750.
DR KEGG; ath:AT3G11750; -.
DR Araport; AT3G11750; -.
DR TAIR; locus:2081496; AT3G11750.
DR eggNOG; ENOG502RZV8; Eukaryota.
DR HOGENOM; CLU_112632_1_0_1; -.
DR InParanoid; Q9SF23; -.
DR OMA; YHGCLVE; -.
DR OrthoDB; 1383549at2759; -.
DR PhylomeDB; Q9SF23; -.
DR BioCyc; ARA:AT3G11750-MON; -.
DR BRENDA; 4.1.2.25; 399.
DR BRENDA; 4.1.2.60; 399.
DR BRENDA; 5.1.99.8; 399.
DR UniPathway; UPA00077; UER00154.
DR EvolutionaryTrace; Q9SF23; -.
DR PRO; PR:Q9SF23; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SF23; baseline and differential.
DR Genevisible; Q9SF23; 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 3D-structure; Direct protein sequencing; Folate biosynthesis; Lyase;
KW Reference proteome.
FT CHAIN 1..146
FT /note="Dihydroneopterin aldolase 1"
FT /id="PRO_0000168294"
FT ACT_SITE 119
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:15165863"
FT BINDING 41
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AC16,
FT ECO:0000305|PubMed:15165863"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AC16,
FT ECO:0000305|PubMed:15165863"
FT BINDING 92..93
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AC16,
FT ECO:0000305|PubMed:15165863"
FT STRAND 23..33
FT /evidence="ECO:0007829|PDB:1SQL"
FT HELIX 39..44
FT /evidence="ECO:0007829|PDB:1SQL"
FT STRAND 46..55
FT /evidence="ECO:0007829|PDB:1SQL"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:1SQL"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:1SQL"
FT HELIX 73..84
FT /evidence="ECO:0007829|PDB:1SQL"
FT HELIX 92..106
FT /evidence="ECO:0007829|PDB:1SQL"
FT STRAND 112..121
FT /evidence="ECO:0007829|PDB:1SQL"
FT STRAND 130..139
FT /evidence="ECO:0007829|PDB:1SQL"
SQ SEQUENCE 146 AA; 16281 MW; 3B7C1D6AF9117770 CRC64;
MHSSLETTAP ATLERRESNL GDKLILKGLK FYGFHGAIAE ERTLGQMFLV DIDAWVSLKK
AGESDNLEDT ISYVDIFSLA KEIVEGSPRN LLETVAELIA SKTLEKFHQI NAVRVKLSKP
NVALIKSTID YLGVDIFRQR NTSSKN
