SWISSPROT: B4SHJ1_STRM5

ID   B4SHJ1_STRM5            Unreviewed;       117 AA.
AC   B4SHJ1;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   16-JAN-2019, entry version 51.
DE   RecName: Full=7,8-dihydroneopterin aldolase {ECO:0000256|RuleBase:RU362079};
DE            EC=4.1.2.25 {ECO:0000256|RuleBase:RU362079};
GN   OrderedLocusNames=Smal_0329 {ECO:0000313|EMBL:ACF50034.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF50034.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF50034.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF50034.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) 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|RuleBase:RU362079};
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-
CC       amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate
CC       from 7,8-dihydroneopterin triphosphate: step 3/4.
CC       {ECO:0000256|RuleBase:RU362079}.
CC   -!- SIMILARITY: Belongs to the DHNA family.
CC       {ECO:0000256|RuleBase:RU362079}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001111; ACF50034.1; -; Genomic_DNA.
DR   RefSeq; WP_012509846.1; NC_011071.1.
DR   STRING; 391008.Smal_0329; -.
DR   EnsemblBacteria; ACF50034; ACF50034; Smal_0329.
DR   KEGG; smt:Smal_0329; -.
DR   eggNOG; ENOG4107ZVW; Bacteria.
DR   eggNOG; COG1539; LUCA.
DR   HOGENOM; HOG000217627; -.
DR   KO; K01633; -.
DR   OMA; GIYEWEK; -.
DR   OrthoDB; 1858654at2; -.
DR   BioCyc; SMAL391008:SMAL_RS01720-MONOMER; -.
DR   UniPathway; UPA00077; UER00154.
DR   Proteomes; UP000001867; 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   InterPro; IPR006156; Dihydroneopterin_aldolase.
DR   InterPro; IPR006157; FolB_dom.
DR   Pfam; PF02152; FolB; 1.
DR   SMART; SM00905; FolB; 1.
DR   TIGRFAMs; TIGR00525; folB; 1.
DR   TIGRFAMs; TIGR00526; folB_dom; 1.
PE   3: Inferred from homology;
DR   PRODOM; B4SHJ1.
DR   SWISS-2DPAGE; B4SHJ1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Folate biosynthesis {ECO:0000256|RuleBase:RU362079};
KW   Lyase {ECO:0000256|RuleBase:RU362079}.
FT   DOMAIN        4    114       FolB. {ECO:0000259|SMART:SM00905}.
SQ   SEQUENCE   117 AA;  13469 MW;  304EFCC40571A7BF CRC64;
     MDKVFIEGLT IDALIGIYDW ERRIRQDLVF DLEMGFDNRR PAASDDIAHT LNYKAVSKRL
     EQFVRESEFG LVETLAERCA QIVLSEFDVK WLRLKLSKPG AVRGARAVGV IIERTRD
//