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Database: UniProt
Entry: I3YFY2_THIV6
LinkDB: I3YFY2_THIV6
Original site: I3YFY2_THIV6 
ID   I3YFY2_THIV6            Unreviewed;       132 AA.
AC   I3YFY2;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=dihydroneopterin aldolase {ECO:0000256|ARBA:ARBA00013043};
DE            EC=4.1.2.25 {ECO:0000256|ARBA:ARBA00013043};
DE   AltName: Full=7,8-dihydroneopterin aldolase {ECO:0000256|ARBA:ARBA00032903};
GN   OrderedLocusNames=Thivi_4077 {ECO:0000313|EMBL:AFL75900.1};
OS   Thiocystis violascens (strain ATCC 17096 / DSM 198 / 6111) (Chromatium
OS   violascens).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thiocystis.
OX   NCBI_TaxID=765911 {ECO:0000313|EMBL:AFL75900.1, ECO:0000313|Proteomes:UP000006062};
RN   [1] {ECO:0000313|EMBL:AFL75900.1, ECO:0000313|Proteomes:UP000006062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17096 / DSM 198 / 6111
RC   {ECO:0000313|Proteomes:UP000006062};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z.,
RA   Frigaard N.-U., Bryant D., Woyke T.;
RT   "Complete sequence of Thiocystis violascens DSM 198.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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   -!- 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}.
CC   -!- SIMILARITY: Belongs to the DHNA family.
CC       {ECO:0000256|ARBA:ARBA00005708}.
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DR   EMBL; CP003154; AFL75900.1; -; Genomic_DNA.
DR   RefSeq; WP_014780286.1; NC_018012.1.
DR   AlphaFoldDB; I3YFY2; -.
DR   STRING; 765911.Thivi_4077; -.
DR   KEGG; tvi:Thivi_4077; -.
DR   eggNOG; COG1539; Bacteria.
DR   HOGENOM; CLU_112632_0_2_6; -.
DR   OrthoDB; 9810587at2; -.
DR   Proteomes; UP000006062; Chromosome.
DR   GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:InterPro.
DR   GO; GO:0006760; P:folic acid-containing compound metabolic process; IEA:InterPro.
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; 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   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006062}.
FT   DOMAIN          4..114
FT                   /note="Dihydroneopterin aldolase/epimerase"
FT                   /evidence="ECO:0000259|SMART:SM00905"
SQ   SEQUENCE   132 AA;  14638 MW;  644F2C507150B71B CRC64;
     MDIVFIRGLR IETIIGIHDW EKHARRPLIL DLEMASDIAR AAATDRIADA LDYDAVTRRL
     VHTVSENRFE LVETLAEHCA ALLREEFGIP WLRLTLNKPG AVGEGVDVGV VIERGERSAN
     KAVGVQPSDA SR
//
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