ID A1D759_NEOFI Unreviewed; 351 AA.
AC A1D759;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 64.
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=NFIA_067200 {ECO:0000313|EMBL:EAW21553.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW21553.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027690; EAW21553.1; -; Genomic_DNA.
DR RefSeq; XP_001263450.1; XM_001263449.1.
DR AlphaFoldDB; A1D759; -.
DR STRING; 331117.A1D759; -.
DR EnsemblFungi; EAW21553; EAW21553; NFIA_067200.
DR GeneID; 4590096; -.
DR KEGG; nfi:NFIA_067200; -.
DR VEuPathDB; FungiDB:NFIA_067200; -.
DR eggNOG; KOG2544; Eukaryota.
DR HOGENOM; CLU_062068_1_0_1; -.
DR OMA; FGQCEVS; -.
DR OrthoDB; 2093080at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:InterPro.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1130.10; -; 2.
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:UP000006702}.
FT DOMAIN 229..336
FT /note="Dihydroneopterin aldolase/epimerase"
FT /evidence="ECO:0000259|SMART:SM00905"
SQ SEQUENCE 351 AA; 38704 MW; 6C82097D63ECB3A7 CRC64;
MAEQRVNVHI PSHPAVLDSV QLRNIQLPLP VAPDPWHRDG KPQPCTASLK LSYSSAIAAA
AADDVSLSLD YGKLYRRLEE DIRNMGKHSL SPTQRMVSAD GSRRDEMMRT EIGQDVRLTA
GIVANCGLGL LDETAAGIRR MSHVHCHPGS RRGSASAEIQ APLAGLSLAS PPIDSVFGQC
EVWLQLPKAL LRAEEGFKYR SVTVWGYRQG DESTALDGER CPVVLEEEFR IDGIRCHCIL
GVNSHERVEK QAVIISLEFK GPGQLAWGST VVDTYQEMTR RVAEQVEETA FQTVEALATF
VARIVTVQFA NERVTVRVEK PSALSFVERS GIEITRSQAF FERSDLEGGR V
//
