ID B1ZQM2_OPITP Unreviewed; 125 AA.
AC B1ZQM2;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=7,8-dihydroneopterin aldolase {ECO:0000256|RuleBase:RU362079};
DE EC=4.1.2.25 {ECO:0000256|RuleBase:RU362079};
GN OrderedLocusNames=Oter_2349 {ECO:0000313|EMBL:ACB75631.1};
OS Opitutus terrae (strain DSM 11246 / JCM 15787 / PB90-1).
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae; Opitutus.
OX NCBI_TaxID=452637 {ECO:0000313|EMBL:ACB75631.1, ECO:0000313|Proteomes:UP000007013};
RN [1] {ECO:0000313|EMBL:ACB75631.1, ECO:0000313|Proteomes:UP000007013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11246 / JCM 15787 / PB90-1
RC {ECO:0000313|Proteomes:UP000007013};
RX PubMed=21398538; DOI=10.1128/JB.00228-11;
RA van Passel M.W., Kant R., Palva A., Copeland A., Lucas S., Lapidus A.,
RA Glavina del Rio T., Pitluck S., Goltsman E., Clum A., Sun H., Schmutz J.,
RA Larimer F.W., Land M.L., Hauser L., Kyrpides N., Mikhailova N.,
RA Richardson P.P., Janssen P.H., de Vos W.M., Smidt H.;
RT "Genome sequence of the verrucomicrobium Opitutus terrae PB90-1, an
RT abundant inhabitant of rice paddy soil ecosystems.";
RL J. Bacteriol. 193:2367-2368(2011).
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}.
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DR EMBL; CP001032; ACB75631.1; -; Genomic_DNA.
DR RefSeq; WP_012375168.1; NC_010571.1.
DR AlphaFoldDB; B1ZQM2; -.
DR STRING; 452637.Oter_2349; -.
DR KEGG; ote:Oter_2349; -.
DR eggNOG; COG1539; Bacteria.
DR HOGENOM; CLU_112632_1_3_0; -.
DR OrthoDB; 9808041at2; -.
DR UniPathway; UPA00077; UER00154.
DR Proteomes; UP000007013; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007013}.
FT DOMAIN 4..117
FT /note="Dihydroneopterin aldolase/epimerase"
FT /evidence="ECO:0000259|SMART:SM00905"
SQ SEQUENCE 125 AA; 14074 MW; 7B195111C8B66CAE CRC64;
MDKLILRELH FVARHGVLPI ETETSQHFSA TLELELPLAP AGETDRLDRT LDYCAVQAVV
RKIIEGTHKK LIETLAESVA RELLLAFPLL VAVTVEITKP RPPVDFQFAG VSVRIRRERS
QLAPR
//
