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Database: UniProt
Entry: K1KJ36_9BURK
LinkDB: K1KJ36_9BURK
Original site: K1KJ36_9BURK 
ID   K1KJ36_9BURK            Unreviewed;       133 AA.
AC   K1KJ36;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 32.
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   ORFNames=HMPREF9465_00602 {ECO:0000313|EMBL:EKB31734.1};
OS   Sutterella wadsworthensis 2_1_59BFAA.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sutterellaceae; Sutterella.
OX   NCBI_TaxID=742823 {ECO:0000313|EMBL:EKB31734.1, ECO:0000313|Proteomes:UP000005835};
RN   [1] {ECO:0000313|EMBL:EKB31734.1, ECO:0000313|Proteomes:UP000005835}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2_1_59BFAA {ECO:0000313|EMBL:EKB31734.1,
RC   ECO:0000313|Proteomes:UP000005835};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA   Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Sutterella wadsworthensis 2_1_59BFAA.";
RL   Submitted (MAY-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKB31734.1}.
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DR   EMBL; ADMG01000017; EKB31734.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1KJ36; -.
DR   STRING; 742823.HMPREF9465_00602; -.
DR   PATRIC; fig|742823.3.peg.603; -.
DR   eggNOG; COG1539; Bacteria.
DR   HOGENOM; CLU_112632_0_1_4; -.
DR   OrthoDB; 8774845at2; -.
DR   Proteomes; UP000005835; Unassembled WGS sequence.
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:UP000005835}.
FT   DOMAIN          16..127
FT                   /note="Dihydroneopterin aldolase/epimerase"
FT                   /evidence="ECO:0000259|SMART:SM00905"
SQ   SEQUENCE   133 AA;  15054 MW;  53DD24DFE94762FB CRC64;
     MNSHITDFLT FQCRKIFVRG LVLDCHIGAY EHEKHRTQKV TFECDVWIPL QDSTSSCDEL
     QDVLNYDLIV GTISDIAQSA HFNLQETLVD AIADKLATLP GVQLLRVSSA KTEAYEHVDA
     VGIEVWRRRP SLP
//
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