GenomeNet

Database: UniProt
Entry: G9Z2X7_9ENTR
LinkDB: G9Z2X7_9ENTR
Original site: G9Z2X7_9ENTR 
ID   G9Z2X7_9ENTR            Unreviewed;       122 AA.
AC   G9Z2X7;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=7,8-dihydroneopterin aldolase {ECO:0000256|RuleBase:RU362079};
DE            EC=4.1.2.25 {ECO:0000256|RuleBase:RU362079};
GN   ORFNames=HMPREF0880_01771 {ECO:0000313|EMBL:EHM49207.1};
OS   Yokenella regensburgei ATCC 43003.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Yokenella.
OX   NCBI_TaxID=1002368 {ECO:0000313|EMBL:EHM49207.1, ECO:0000313|Proteomes:UP000003044};
RN   [1] {ECO:0000313|EMBL:EHM49207.1, ECO:0000313|Proteomes:UP000003044}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43003 {ECO:0000313|EMBL:EHM49207.1,
RC   ECO:0000313|Proteomes:UP000003044};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-2011) 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-amino-
CC       4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-
CC       dihydroneopterin triphosphate: step 3/4.
CC       {ECO:0000256|RuleBase:RU362079}.
CC   -!- SUBUNIT: Homooctamer. {ECO:0000256|ARBA:ARBA00011823}.
CC   -!- SIMILARITY: Belongs to the DHNA family. {ECO:0000256|ARBA:ARBA00005708,
CC       ECO:0000256|RuleBase:RU362079}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHM49207.1}.
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; AGCL01000028; EHM49207.1; -; Genomic_DNA.
DR   RefSeq; WP_006818252.1; NZ_JH417873.1.
DR   AlphaFoldDB; G9Z2X7; -.
DR   STRING; 1002368.HMPREF0880_01771; -.
DR   GeneID; 66904795; -.
DR   PATRIC; fig|1002368.3.peg.1624; -.
DR   HOGENOM; CLU_112632_0_2_6; -.
DR   UniPathway; UPA00077; UER00154.
DR   Proteomes; UP000003044; Unassembled WGS sequence.
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|RuleBase:RU362079};
KW   Lyase {ECO:0000256|RuleBase:RU362079}.
FT   DOMAIN          4..114
FT                   /note="Dihydroneopterin aldolase/epimerase"
FT                   /evidence="ECO:0000259|SMART:SM00905"
SQ   SEQUENCE   122 AA;  13481 MW;  C55EFF937AF09A79 CRC64;
     MDIVFIEQLS VITTIGVYDW EQTIEQKLVF DIEMAWDNQK AAASDNVDDC LSYADISEAV
     VGHVEGARFA LVERVAEEVA SLLLSRFNSP WVRIKVSKPG AVARAANVGV VIERSQTLKA
     EK
//
DBGET integrated database retrieval system