(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BHM9_GEOS0

ID   A0A0F6BHM9_GEOS0        Unreviewed;       126 AA.
AC   A0A0F6BHM9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   16-JAN-2019, entry version 22.
DE   RecName: Full=7,8-dihydroneopterin aldolase {ECO:0000256|RuleBase:RU362079};
DE            EC=4.1.2.25 {ECO:0000256|RuleBase:RU362079};
GN   OrderedLocusNames=GY4MC1_0074 {ECO:0000313|EMBL:ADP72930.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72930.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP72930.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72930.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) 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}.
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DR   EMBL; CP002293; ADP72930.1; -; Genomic_DNA.
DR   RefSeq; WP_003247485.1; NC_014650.1.
DR   EnsemblBacteria; ADP72930; ADP72930; GY4MC1_0074.
DR   GeneID; 29237304; -.
DR   KEGG; gmc:GY4MC1_0074; -.
DR   KO; K01633; -.
DR   OMA; FYAYHGV; -.
DR   OrthoDB; 1858654at2; -.
DR   BioCyc; GSP581103:G1GOQ-87-MONOMER; -.
DR   UniPathway; UPA00077; UER00154.
DR   Proteomes; UP000002034; 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; A0A0F6BHM9.
DR   SWISS-2DPAGE; A0A0F6BHM9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Folate biosynthesis {ECO:0000256|RuleBase:RU362079};
KW   Lyase {ECO:0000256|RuleBase:RU362079, ECO:0000313|EMBL:ADP72930.1}.
FT   DOMAIN       11    124       FolB. {ECO:0000259|SMART:SM00905}.
SQ   SEQUENCE   126 AA;  14528 MW;  6BFDFDA2F9015DE8 CRC64;
     MEKEWRTIDK IYLHRMEFYG YHGVLPEENV LGQRFIVDAI LETDLQKAGK SDQLNDTINY
     AEVYDICRNV VEKRRFSLIE AVAETIAEQI LSSFPTVARC TIKVTKPNPP IKGHYESVAV
     EIVRGR
//

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