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Entry: A0A0F2MJP6_SPOSC
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ID   A0A0F2MJP6_SPOSC        Unreviewed;       300 AA.
AC   A0A0F2MJP6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=SPSK_06514 {ECO:0000313|EMBL:KJR89928.1};
OS   Sporothrix schenckii 1099-18.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX   NCBI_TaxID=1397361 {ECO:0000313|EMBL:KJR89928.1, ECO:0000313|Proteomes:UP000033710};
RN   [1] {ECO:0000313|EMBL:KJR89928.1, ECO:0000313|Proteomes:UP000033710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1099-18 {ECO:0000313|EMBL:KJR89928.1,
RC   ECO:0000313|Proteomes:UP000033710};
RX   PubMed=25351875; DOI=10.1186/1471-2164-15-943;
RA   Teixeira M.M., de Almeida L.G., Kubitschek-Barreira P., Alves F.L.,
RA   Kioshima E.S., Abadio A.K., Fernandes L., Derengowski L.S., Ferreira K.S.,
RA   Souza R.C., Ruiz J.C., de Andrade N.C., Paes H.C., Nicola A.M.,
RA   Albuquerque P., Gerber A.L., Martins V.P., Peconick L.D., Neto A.V.,
RA   Chaucanez C.B., Silva P.A., Cunha O.L., de Oliveira F.F., dos Santos T.C.,
RA   Barros A.L., Soares M.A., de Oliveira L.M., Marini M.M.,
RA   Villalobos-Duno H., Cunha M.M., de Hoog S., da Silveira J.F., Henrissat B.,
RA   Nino-Vega G.A., Cisalpino P.S., Mora-Montes H.M., Almeida S.R.,
RA   Stajich J.E., Lopes-Bezerra L.M., Vasconcelos A.T., Felipe M.S.;
RT   "Comparative genomics of the major fungal agents of human and animal
RT   Sporotrichosis: Sporothrix schenckii and Sporothrix brasiliensis.";
RL   BMC Genomics 15:943-943(2014).
RN   [2] {ECO:0000313|EMBL:KJR89928.1, ECO:0000313|Proteomes:UP000033710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1099-18 {ECO:0000313|EMBL:KJR89928.1,
RC   ECO:0000313|Proteomes:UP000033710};
RX   PubMed=25480940;
RA   Teixeira Mde M., Rodrigues A.M., Tsui C.K., de Almeida L.G.,
RA   Van Diepeningen A.D., van den Ende B.G., Fernandes G.F., Kano R.,
RA   Hamelin R.C., Lopes-Bezerra L.M., Vasconcelos A.T., de Hoog S.,
RA   de Camargo Z.P., Felipe M.S.;
RT   "Asexual propagation of a virulent clone complex in a human and feline
RT   outbreak of sporotrichosis.";
RL   Eukaryot. Cell 14:158-169(2015).
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:KJR89928.1}.
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DR   EMBL; AXCR01000001; KJR89928.1; -; Genomic_DNA.
DR   RefSeq; XP_016592604.1; XM_016733218.1.
DR   AlphaFoldDB; A0A0F2MJP6; -.
DR   GeneID; 27668495; -.
DR   KEGG; ssck:SPSK_06514; -.
DR   VEuPathDB; FungiDB:SPSK_06514; -.
DR   OrthoDB; 2093080at2759; -.
DR   Proteomes; UP000033710; Unassembled WGS sequence.
DR   GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; 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   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   Kinase {ECO:0000313|EMBL:KJR89928.1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Transferase {ECO:0000313|EMBL:KJR89928.1}.
FT   DOMAIN          183..295
FT                   /note="Dihydroneopterin aldolase/epimerase"
FT                   /evidence="ECO:0000259|SMART:SM00905"
FT   REGION          113..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   300 AA;  32025 MW;  F4CAD4F7D2D6B156 CRC64;
     MPQPTAWDVQ AAIGEPRAVI RVRGLQATLG PGAGQDAWGR NGRPQPAVLS AEAVLAAPFP
     EAANTDQVAG DTVHYGTLSK AVLKSLKRWD EERPPTGLLH VLDGLWIDLT GRMATGAKPS
     SPDAPSQDPS QNPPLLSASV VRSLSVTVLL PKATLVGEGV SLTSAGVLAR AAKGTAPIAS
     NTLRLHRLRV PTLVGVHPHE RTAKQAVVAD IALDRFTEYE DVYTRLEAFV VQILETSEFE
     TLEALATHIA RLILLRFRPN GPFPGPDLPP WYVHVSLEKP IAVPSADAPV VEVRMGAEHL
//
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