(data stored in SCRATCH zone)

SWISSPROT: C8W3T5_DESAS

ID   C8W3T5_DESAS            Unreviewed;       121 AA.
AC   C8W3T5;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, 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=Dtox_0236 {ECO:0000313|EMBL:ACV61189.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61189.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61189.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
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}.
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DR   EMBL; CP001720; ACV61189.1; -; Genomic_DNA.
DR   RefSeq; WP_015755910.1; NC_013216.1.
DR   STRING; 485916.Dtox_0236; -.
DR   EnsemblBacteria; ACV61189; ACV61189; Dtox_0236.
DR   KEGG; dae:Dtox_0236; -.
DR   eggNOG; ENOG4105KRF; Bacteria.
DR   eggNOG; COG1539; LUCA.
DR   HOGENOM; HOG000217628; -.
DR   KO; K01633; -.
DR   OMA; FYAYHGV; -.
DR   OrthoDB; 1858654at2; -.
DR   BioCyc; DACE485916:G1GFV-241-MONOMER; -.
DR   UniPathway; UPA00077; UER00154.
DR   Proteomes; UP000002217; 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; C8W3T5.
DR   SWISS-2DPAGE; C8W3T5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Folate biosynthesis {ECO:0000256|RuleBase:RU362079};
KW   Lyase {ECO:0000256|RuleBase:RU362079};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217}.
FT   DOMAIN        5    117       FolB. {ECO:0000259|SMART:SM00905}.
SQ   SEQUENCE   121 AA;  13720 MW;  6FB3B7FF64598BCF CRC64;
     MSDKIILSGL DFYGYHGVLP EEQRLGQKFI IDLELSLSLR EAGIKDDPDL TVNYARVFET
     VREVVVGKPF FLIEALAEAI AFKVLKNFSI EKVLVRVRKP QAPVPGCFEH MAVEITREKE
     V
//

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