ID A0A0P1GMI6_9RHOB Unreviewed; 312 AA.
AC A0A0P1GMI6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=TRN7648_01004 {ECO:0000313|EMBL:CUH76570.1};
OS Tropicibacter naphthalenivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Tropicibacter.
OX NCBI_TaxID=441103 {ECO:0000313|EMBL:CUH76570.1, ECO:0000313|Proteomes:UP000054935};
RN [1] {ECO:0000313|EMBL:CUH76570.1, ECO:0000313|Proteomes:UP000054935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7648 {ECO:0000313|EMBL:CUH76570.1,
RC ECO:0000313|Proteomes:UP000054935};
RG Swine Surveillance;
RL Submitted (SEP-2015) 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; CYSE01000002; CUH76570.1; -; Genomic_DNA.
DR RefSeq; WP_058246549.1; NZ_FWXX01000002.1.
DR AlphaFoldDB; A0A0P1GMI6; -.
DR STRING; 441103.TRN7648_01004; -.
DR OrthoDB; 7678026at2; -.
DR Proteomes; UP000054935; 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 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:UP000054935}.
FT DOMAIN 28..136
FT /note="Dihydroneopterin aldolase/epimerase"
FT /evidence="ECO:0000259|SMART:SM00905"
SQ SEQUENCE 312 AA; 34266 MW; 885AD360499261CA CRC64;
MASEIRLAFA HPSERAIATA GDAPRDRISV RDHVVEVEIG AFQAERGTKQ RVQFNVVVEV
IPVTGVLDDD VDLILSYDRV TEAIAHELAA ERLNLLETLA ERIAERILLE PQALRAFVRI
EKLDRGPGAL GVEIVRTKRD YGGHLETLAE EVAQEQPHPR VVYLSNAAIE DPRLTAWVDE
LASRRAPVIL CVGRPDLPAP QTGHAMTQRR VDLLSLEQNG WVLAARDHRC KVVATRTELD
WAMKNGQICV WAPSKIVLDA TQGPQAQPRD SVALAAWFAG EMEACELVVI GEDLPEGAAT
PARAVTPDDA LF
//
