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Database: UniProt
Entry: T2J2I4_CROWT
LinkDB: T2J2I4_CROWT
Original site: T2J2I4_CROWT 
ID   T2J2I4_CROWT            Unreviewed;       127 AA.
AC   T2J2I4;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=7,8-dihydroneopterin aldolase {ECO:0000256|RuleBase:RU362079};
DE            EC=4.1.2.25 {ECO:0000256|RuleBase:RU362079};
GN   ORFNames=CWATWH0005_2088 {ECO:0000313|EMBL:CCQ58635.1};
OS   Crocosphaera watsonii WH 0005.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Aphanothecaceae; Crocosphaera.
OX   NCBI_TaxID=423472 {ECO:0000313|EMBL:CCQ58635.1, ECO:0000313|Proteomes:UP000017981};
RN   [1] {ECO:0000313|EMBL:CCQ58635.1, ECO:0000313|Proteomes:UP000017981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH 0005 {ECO:0000313|EMBL:CCQ58635.1,
RC   ECO:0000313|Proteomes:UP000017981};
RA   Bench S.;
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CCQ58635.1, ECO:0000313|Proteomes:UP000017981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH 0005 {ECO:0000313|EMBL:CCQ58635.1,
RC   ECO:0000313|Proteomes:UP000017981};
RA   Bench S.R., Heller P., Frank I., Arciniega M., Shilova I.N., Zehr J.P.;
RT   "Whole genome comparison of six Crocosphaera watsonii strains with
RT   differing phenotypes.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-
CC       hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}.
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         ECO:0000256|RuleBase:RU362079};
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, ECO:0000256|RuleBase:RU362079}.
CC   -!- SIMILARITY: Belongs to the DHNA family. {ECO:0000256|ARBA:ARBA00005708,
CC       ECO:0000256|RuleBase:RU362079}.
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:CCQ58635.1}.
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DR   EMBL; CAQL01001059; CCQ58635.1; -; Genomic_DNA.
DR   AlphaFoldDB; T2J2I4; -.
DR   UniPathway; UPA00077; UER00154.
DR   Proteomes; UP000017981; Unassembled WGS sequence.
DR   GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00534; DHNA_DHNTPE; 1.
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; TIGR00525; folB; 1.
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   ECO:0000256|RuleBase:RU362079};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU362079}.
FT   DOMAIN          11..123
FT                   /note="Dihydroneopterin aldolase/epimerase"
FT                   /evidence="ECO:0000259|SMART:SM00905"
SQ   SEQUENCE   127 AA;  14203 MW;  ED2E2EBFAF3E5A1B CRC64;
     MKVTNTQMDF IEVTGIRCYG YTGYLPEEQV LGQWFEVDLT LGADLTNAGT SDNLDDTSDY
     RQAIAIVKHH IKTTKVALIE RLTEIIAQEI LALPNINQVR VRLTKVSPPI PDFAGKITVD
     ITRINKS
//
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