ID A0A067DC52_CITSI Unreviewed; 134 AA.
AC A0A067DC52;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=7,8-dihydroneopterin aldolase {ECO:0000256|RuleBase:RU362079};
DE EC=4.1.2.25 {ECO:0000256|RuleBase:RU362079};
GN ORFNames=CISIN_1g032783mg {ECO:0000313|EMBL:KDO36607.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO36607.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO36607.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-
CC hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}.
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:0000256|ARBA:ARBA00001353,
CC ECO:0000256|RuleBase:RU362079};
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 {ECO:0000256|ARBA:ARBA00005013, ECO:0000256|RuleBase:RU362079}.
CC -!- SIMILARITY: Belongs to the DHNA family. {ECO:0000256|ARBA:ARBA00005708,
CC ECO:0000256|RuleBase:RU362079}.
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DR EMBL; KK793770; KDO36607.1; -; Genomic_DNA.
DR EMBL; KK793770; KDO36608.1; -; Genomic_DNA.
DR RefSeq; XP_006481623.1; XM_006481560.2.
DR RefSeq; XP_006481624.1; XM_006481561.2.
DR STRING; 2711.A0A067DC52; -.
DR PaxDb; 2711-XP_006481623-1; -.
DR GeneID; 102607659; -.
DR KEGG; cit:102607659; -.
DR eggNOG; ENOG502RZV8; Eukaryota.
DR OrthoDB; 444536at2759; -.
DR UniPathway; UPA00077; UER00154.
DR Proteomes; UP000027120; Unassembled WGS sequence.
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-UniRule.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniRule.
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 NCBIfam; TIGR00525; folB; 1.
DR NCBIfam; TIGR00526; folB_dom; 1.
DR PANTHER; PTHR42844; DIHYDRONEOPTERIN ALDOLASE 1-RELATED; 1.
DR PANTHER; PTHR42844:SF1; DIHYDRONEOPTERIN ALDOLASE 1-RELATED; 1.
DR Pfam; PF02152; FolB; 1.
DR SMART; SM00905; FolB; 1.
DR SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 1.
PE 3: Inferred from homology;
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909,
KW ECO:0000256|RuleBase:RU362079};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU362079};
KW Reference proteome {ECO:0000313|Proteomes:UP000027120}.
FT DOMAIN 12..125
FT /note="Dihydroneopterin aldolase/epimerase"
FT /evidence="ECO:0000259|SMART:SM00905"
SQ SEQUENCE 134 AA; 15028 MW; 8D74E2DE1134F90F CRC64;
MEDIEIMKGD KLILRGLRFH GFHGVKKEER TLGQKFVVDV DAWMDLRKAG KTDLLADTIS
YTAIYRIVKE IMEGPPHNLL ESVAELIAST TLTKYPQISA VRVKVGKPHV AVEGSLDYLG
IEILRHRSVD APNC
//
