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Database: UniProt
Entry: A0A0R0E6R7_9GAMM
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ID   A0A0R0E6R7_9GAMM        Unreviewed;       117 AA.
AC   A0A0R0E6R7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=7,8-dihydroneopterin aldolase {ECO:0000256|RuleBase:RU362079};
DE            EC=4.1.2.25 {ECO:0000256|RuleBase:RU362079};
GN   Name=folB {ECO:0000313|EMBL:ALJ26540.1};
GN   ORFNames=ABB33_06510 {ECO:0000313|EMBL:KRG85764.1}, AOT14_00780
GN   {ECO:0000313|EMBL:ALJ26540.1};
OS   Stenotrophomonas acidaminiphila.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=128780 {ECO:0000313|EMBL:KRG85764.1, ECO:0000313|Proteomes:UP000050958};
RN   [1] {ECO:0000313|EMBL:ALJ26540.1, ECO:0000313|Proteomes:UP000061010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZAC14D2_NAIMI4_2 {ECO:0000313|EMBL:ALJ26540.1,
RC   ECO:0000313|Proteomes:UP000061010};
RX   PubMed=26659678;
RA   Vinuesa P., Ochoa-Sanchez L.E.;
RT   "Complete Genome Sequencing of Stenotrophomonas acidaminiphila
RT   ZAC14D2_NAIMI4_2, a Multidrug-Resistant Strain Isolated from Sediments of a
RT   Polluted River in Mexico, Uncovers New Antibiotic Resistance Genes and a
RT   Novel Class-II Lasso Peptide Biosynthesis Gene Cluster.";
RL   Genome Announc. 3:e01433-15(2015).
RN   [2] {ECO:0000313|EMBL:KRG85764.1, ECO:0000313|Proteomes:UP000050958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 13310 {ECO:0000313|EMBL:KRG85764.1,
RC   ECO:0000313|Proteomes:UP000050958};
RA   Patil P.P., Midha S., Patil P.B.;
RT   "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL   Submitted (MAY-2015) 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}.
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DR   EMBL; CP012900; ALJ26540.1; -; Genomic_DNA.
DR   EMBL; LDJO01000021; KRG85764.1; -; Genomic_DNA.
DR   RefSeq; WP_054661414.1; NZ_RZNW01000042.1.
DR   AlphaFoldDB; A0A0R0E6R7; -.
DR   GeneID; 78388115; -.
DR   KEGG; sacz:AOT14_00780; -.
DR   PATRIC; fig|128780.6.peg.75; -.
DR   OrthoDB; 9810587at2; -.
DR   UniPathway; UPA00077; UER00154.
DR   Proteomes; UP000050958; Unassembled WGS sequence.
DR   Proteomes; UP000061010; 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}.
FT   DOMAIN          4..114
FT                   /note="Dihydroneopterin aldolase/epimerase"
FT                   /evidence="ECO:0000259|SMART:SM00905"
SQ   SEQUENCE   117 AA;  13316 MW;  CBF9820664BC0012 CRC64;
     MDKVFIEGLE IEALIGIYDW ERRIRQTLVF DLEMGFDNRR PAATDDIADT LNYKAVSRRL
     QEYVGGSDFG LVETLAERCA AIVLDEFDVR WLRLKLSKPG AVRGARAVGV IIERERG
//
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