ID Q8CZR7_YERPE Unreviewed; 120 AA.
AC Q8CZR7;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=7,8-dihydroneopterin aldolase {ECO:0000256|RuleBase:RU362079};
DE EC=4.1.2.25 {ECO:0000256|RuleBase:RU362079};
GN OrderedLocusNames=y3531 {ECO:0000313|EMBL:AAM87079.1};
OS Yersinia pestis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632 {ECO:0000313|EMBL:AAM87079.1, ECO:0000313|Proteomes:UP000002490};
RN [1] {ECO:0000313|EMBL:AAM87079.1, ECO:0000313|Proteomes:UP000002490}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis
RC {ECO:0000313|Proteomes:UP000002490};
RX PubMed=12142430; DOI=10.1128/JB.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G.III., Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plana G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [2] {ECO:0007829|PDB:7SU7}
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 2-120.
RA Bourne C.R.;
RT "Dihydroneopterin aldolase (DHNA) from Yersinia pestis co-crystallized with
RT product.";
RL Submitted (NOV-2021) to the PDB data bank.
RN [3] {ECO:0007829|PDB:7SU4}
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 2-120.
RA Bourne C.R., Tan A.;
RT "Dihydroneopterin aldolase (DHNA) Tyr53Phe from Yersinia pestis co-
RT crystallized with 7,8-dihydroneopterin.";
RL Submitted (NOV-2021) to the PDB data bank.
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 -!- SUBUNIT: Homooctamer. {ECO:0000256|ARBA:ARBA00011823}.
CC -!- SIMILARITY: Belongs to the DHNA family. {ECO:0000256|ARBA:ARBA00005708,
CC ECO:0000256|RuleBase:RU362079}.
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DR EMBL; AE009952; AAM87079.1; -; Genomic_DNA.
DR PDB; 7SU4; X-ray; 1.78 A; A/B/C/D=2-120.
DR PDB; 7SU7; X-ray; 2.09 A; A/B/C/D=2-120.
DR PDBsum; 6OJO; -.
DR AlphaFoldDB; Q8CZR7; -.
DR SMR; Q8CZR7; -.
DR DNASU; 1148478; -.
DR KEGG; ypk:y3531; -.
DR HOGENOM; CLU_112632_0_2_6; -.
DR UniPathway; UPA00077; UER00154.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:7SU4, ECO:0007829|PDB:7SU7};
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909,
KW ECO:0000256|RuleBase:RU362079}; Kinase {ECO:0000313|EMBL:AAM87079.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU362079};
KW Transferase {ECO:0000313|EMBL:AAM87079.1}.
FT DOMAIN 5..115
FT /note="Dihydroneopterin aldolase/epimerase"
FT /evidence="ECO:0000259|SMART:SM00905"
SQ SEQUENCE 120 AA; 13522 MW; 2B229113DEE925ED CRC64;
MMDIVFIEEL SVITTIGVYD WEQTIQQKLV FDIEMGWDNR KAAGSDDVND CLSYADISEA
VIQHVGSQRF ALVERVAEEV AELLLRRFNS PWVRIKVSKP GAVAQAKNVG VIIERGQRLS
//
