FOLX_ECOLI
ID FOLX_ECOLI Reviewed; 120 AA.
AC P0AC19; P77796; P80449;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Dihydroneopterin triphosphate 2'-epimerase {ECO:0000303|PubMed:9182560};
DE EC=5.1.99.7 {ECO:0000269|PubMed:9182560, ECO:0000269|PubMed:9651328};
DE AltName: Full=D-erythro-7,8-dihydroneopterin triphosphate epimerase;
GN Name=folX; OrderedLocusNames=b2303, JW2300;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=K12 / RR28;
RX PubMed=9006053; DOI=10.1128/jb.179.3.949-951.1997;
RA Haussmann C., Rohdich F., Lottspeich F., Eberhardt S., Scheuring J.,
RA Mackamul S., Bacher A.;
RT "Dihydroneopterin triphosphate epimerase of Escherichia coli: purification,
RT genetic cloning, and expression.";
RL J. Bacteriol. 179:949-951(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=9182560; DOI=10.1074/jbc.272.24.15323;
RA Ahn C., Byun J., Yim J.;
RT "Purification, cloning, and functional expression of dihydroneopterin
RT triphosphate 2'-epimerase from Escherichia coli.";
RL J. Biol. Chem. 272:15323-15328(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 2-22.
RC STRAIN=DSM 613;
RA Haussmann C., Bacher A.;
RL Submitted (MAY-1995) to UniProtKB.
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES,
RP DISRUPTION PHENOTYPE, AND REACTION MECHANISM.
RX PubMed=9651328; DOI=10.1074/jbc.273.28.17418;
RA Haussmann C., Rohdich F., Schmidt E., Bacher A., Richter G.;
RT "Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic
RT similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin
RT aldolase.";
RL J. Biol. Chem. 273:17418-17424(1998).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=19897652; DOI=10.1128/jb.01198-09;
RA Pribat A., Blaby I.K., Lara-Nunez A., Gregory J.F., de Crecy-Lagard V.,
RA Hanson A.D.;
RT "FolX and FolM are essential for tetrahydromonapterin synthesis in
RT Escherichia coli and Pseudomonas aeruginosa.";
RL J. Bacteriol. 192:475-482(2010).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), AND SUBUNIT.
RX PubMed=10378270; DOI=10.1016/s0969-2126(99)80067-7;
RA Ploom T., Haussmann C., Hof P., Steinbacher S., Bacher A., Richardson J.,
RA Huber R.;
RT "Crystal structure of 7,8-dihydroneopterin triphosphate epimerase.";
RL Structure 7:509-516(1999).
CC -!- FUNCTION: Catalyzes the epimerization of carbon 2' of the side chain of
CC 7,8-dihydroneopterin triphosphate (H2NTP) to form 7,8-dihydromonapterin
CC triphosphate (H2MTP) (PubMed:9182560) (PubMed:9651328). Is required for
CC tetrahydromonapterin biosynthesis, a major pterin in E.coli
CC (PubMed:19897652). {ECO:0000269|PubMed:19897652,
CC ECO:0000269|PubMed:9182560, ECO:0000269|PubMed:9651328}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7,8-dihydroneopterin 3'-triphosphate = 7,8-dihydromonapterin
CC 3'-triphosphate; Xref=Rhea:RHEA:28346, ChEBI:CHEBI:58462,
CC ChEBI:CHEBI:61186; EC=5.1.99.7; Evidence={ECO:0000269|PubMed:9182560,
CC ECO:0000269|PubMed:9651328};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13 uM for 7,8-dihydroneopterin triphosphate
CC {ECO:0000269|PubMed:9651328};
CC KM=149 uM for 7,8-dihydroneopterin {ECO:0000269|PubMed:9651328};
CC KM=66 uM for 7,8-dihydromonapterin {ECO:0000269|PubMed:9651328};
CC Vmax=480 umol/h/mg enzyme for the epimerization of 7,8-
CC dihydroneopterin triphosphate {ECO:0000269|PubMed:9651328};
CC Vmax=0.95 umol/h/mg enzyme for the epimerization of 7,8-
CC dihydroneopterin {ECO:0000269|PubMed:9651328};
CC Vmax=0.67 umol/h/mg enzyme for the epimerization of 7,8-
CC dihydromonapterin {ECO:0000269|PubMed:9651328};
CC -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:10378270,
CC ECO:0000269|PubMed:9651328}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show no detectable growth
CC defect on complete and minimal medium (PubMed:9651328). The folX
CC deletion selectively eliminates monapterin production and secretion,
CC but has no effect on the intra- and extracellular folate profiles
CC (PubMed:19897652). {ECO:0000269|PubMed:19897652,
CC ECO:0000269|PubMed:9651328}.
CC -!- SIMILARITY: Belongs to the DHNA family. {ECO:0000305}.
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DR EMBL; X96709; CAA65471.1; -; Genomic_DNA.
DR EMBL; U47639; AAB47972.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16140.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75363.1; -; Genomic_DNA.
DR PIR; E65002; E65002.
DR RefSeq; NP_416806.1; NC_000913.3.
DR RefSeq; WP_000068457.1; NZ_STEB01000008.1.
DR PDB; 1B9L; X-ray; 2.90 A; A/B/C/D/E/F/G/H=1-120.
DR PDBsum; 1B9L; -.
DR AlphaFoldDB; P0AC19; -.
DR SMR; P0AC19; -.
DR BioGRID; 4260518; 7.
DR DIP; DIP-9679N; -.
DR IntAct; P0AC19; 3.
DR STRING; 511145.b2303; -.
DR jPOST; P0AC19; -.
DR PaxDb; P0AC19; -.
DR PRIDE; P0AC19; -.
DR EnsemblBacteria; AAC75363; AAC75363; b2303.
DR EnsemblBacteria; BAA16140; BAA16140; BAA16140.
DR GeneID; 66673814; -.
DR GeneID; 946781; -.
DR KEGG; ecj:JW2300; -.
DR KEGG; eco:b2303; -.
DR PATRIC; fig|1411691.4.peg.4431; -.
DR EchoBASE; EB4011; -.
DR eggNOG; COG1539; Bacteria.
DR HOGENOM; CLU_112632_0_0_6; -.
DR InParanoid; P0AC19; -.
DR OMA; DHALNYR; -.
DR PhylomeDB; P0AC19; -.
DR BioCyc; EcoCyc:H2NTPEPIM-MON; -.
DR BioCyc; MetaCyc:H2NTPEPIM-MON; -.
DR BRENDA; 5.1.99.7; 2026.
DR BRENDA; 5.1.99.8; 2026.
DR SABIO-RK; P0AC19; -.
DR EvolutionaryTrace; P0AC19; -.
DR PRO; PR:P0AC19; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:InterPro.
DR GO; GO:0008719; F:dihydroneopterin triphosphate 2'-epimerase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0006760; P:folic acid-containing compound metabolic process; IEA:InterPro.
DR GO; GO:0042559; P:pteridine-containing compound biosynthetic process; IMP:EcoCyc.
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 PANTHER; PTHR42844; PTHR42844; 1.
DR Pfam; PF02152; FolB; 1.
DR SMART; SM00905; FolB; 1.
DR TIGRFAMs; TIGR00526; folB_dom; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Isomerase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9182560, ECO:0000269|Ref.6"
FT CHAIN 2..120
FT /note="Dihydroneopterin triphosphate 2'-epimerase"
FT /id="PRO_0000168295"
FT CONFLICT 27..30
FT /note="NNRQ -> KQPS (in Ref. 2; AAB47972)"
FT /evidence="ECO:0000305"
FT CONFLICT 48..49
FT /note="SE -> RQ (in Ref. 2; AAB47972)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="L -> M (in Ref. 2; AAB47972)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="R -> A (in Ref. 2; AAB47972)"
FT /evidence="ECO:0000305"
FT STRAND 5..19
FT /evidence="ECO:0007829|PDB:1B9L"
FT HELIX 23..27
FT /evidence="ECO:0007829|PDB:1B9L"
FT STRAND 30..41
FT /evidence="ECO:0007829|PDB:1B9L"
FT HELIX 42..46
FT /evidence="ECO:0007829|PDB:1B9L"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1B9L"
FT HELIX 57..69
FT /evidence="ECO:0007829|PDB:1B9L"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:1B9L"
FT HELIX 76..87
FT /evidence="ECO:0007829|PDB:1B9L"
FT STRAND 94..103
FT /evidence="ECO:0007829|PDB:1B9L"
FT STRAND 109..119
FT /evidence="ECO:0007829|PDB:1B9L"
SQ SEQUENCE 120 AA; 14082 MW; 5DDFF76540827ED6 CRC64;
MAQPAAIIRI KNLRLRTFIG IKEEEINNRQ DIVINVTIHY PADKARTSED INDALNYRTV
TKNIIQHVEN NRFSLLEKLT QDVLDIAREH HWVTYAEVEI DKLHALRYAD SVSMTLSWQR
