FOLD_PSEAE
ID FOLD_PSEAE Reviewed; 284 AA.
AC Q9I2U6;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Bifunctional protein FolD {ECO:0000255|HAMAP-Rule:MF_01576};
DE Includes:
DE RecName: Full=Methylenetetrahydrofolate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01576};
DE EC=1.5.1.5 {ECO:0000255|HAMAP-Rule:MF_01576};
DE Includes:
DE RecName: Full=Methenyltetrahydrofolate cyclohydrolase {ECO:0000255|HAMAP-Rule:MF_01576};
DE EC=3.5.4.9 {ECO:0000255|HAMAP-Rule:MF_01576};
GN Name=folD {ECO:0000255|HAMAP-Rule:MF_01576}; OrderedLocusNames=PA1796;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBUNIT.
RX PubMed=22558288; DOI=10.1371/journal.pone.0035973;
RA Eadsforth T.C., Gardiner M., Maluf F.V., McElroy S., James D., Frearson J.,
RA Gray D., Hunter W.N.;
RT "Assessment of Pseudomonas aeruginosa N5,N10-methylenetetrahydrofolate
RT dehydrogenase-cyclohydrolase as a potential antibacterial drug target.";
RL PLoS ONE 7:E35973-E35973(2012).
CC -!- FUNCTION: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to
CC 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-
CC methenyltetrahydrofolate to 10-formyltetrahydrofolate.
CC {ECO:0000255|HAMAP-Rule:MF_01576, ECO:0000269|PubMed:22558288}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-
CC methenyltetrahydrofolate + NADPH; Xref=Rhea:RHEA:22812,
CC ChEBI:CHEBI:15636, ChEBI:CHEBI:57455, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.5.1.5; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01576, ECO:0000269|PubMed:22558288};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,10-methenyltetrahydrofolate + H2O = (6S)-10-
CC formyltetrahydrofolate + H(+); Xref=Rhea:RHEA:23700,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57454,
CC ChEBI:CHEBI:57455; EC=3.5.4.9; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01576, ECO:0000269|PubMed:22558288};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000255|HAMAP-Rule:MF_01576}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01576,
CC ECO:0000269|PubMed:22558288}.
CC -!- SIMILARITY: Belongs to the tetrahydrofolate
CC dehydrogenase/cyclohydrolase family. {ECO:0000255|HAMAP-Rule:MF_01576}.
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DR EMBL; AE004091; AAG05185.1; -; Genomic_DNA.
DR PIR; H83421; H83421.
DR RefSeq; NP_250487.1; NC_002516.2.
DR RefSeq; WP_003087898.1; NZ_QZGE01000003.1.
DR PDB; 4A5O; X-ray; 2.20 A; A/B/C/D=1-284.
DR PDBsum; 4A5O; -.
DR AlphaFoldDB; Q9I2U6; -.
DR SMR; Q9I2U6; -.
DR STRING; 287.DR97_90; -.
DR PaxDb; Q9I2U6; -.
DR PRIDE; Q9I2U6; -.
DR EnsemblBacteria; AAG05185; AAG05185; PA1796.
DR GeneID; 880636; -.
DR KEGG; pae:PA1796; -.
DR PATRIC; fig|208964.12.peg.1863; -.
DR PseudoCAP; PA1796; -.
DR HOGENOM; CLU_034045_2_1_6; -.
DR InParanoid; Q9I2U6; -.
DR OMA; HIVGRPM; -.
DR PhylomeDB; Q9I2U6; -.
DR BioCyc; PAER208964:G1FZ6-1828-MON; -.
DR BRENDA; 3.5.4.9; 5087.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; IBA:GO_Central.
DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IBA:GO_Central.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IBA:GO_Central.
DR CDD; cd01080; NAD_bind_m-THF_DH_Cyclohyd; 1.
DR HAMAP; MF_01576; THF_DHG_CYH; 1.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000672; THF_DH/CycHdrlase.
DR InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom.
DR InterPro; IPR020867; THF_DH/CycHdrlase_CS.
DR InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom.
DR Pfam; PF00763; THF_DHG_CYH; 1.
DR Pfam; PF02882; THF_DHG_CYH_C; 1.
DR PRINTS; PR00085; THFDHDRGNASE.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR PROSITE; PS00766; THF_DHG_CYH_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Histidine biosynthesis; Hydrolase;
KW Methionine biosynthesis; Multifunctional enzyme; NADP;
KW One-carbon metabolism; Oxidoreductase; Purine biosynthesis;
KW Reference proteome.
FT CHAIN 1..284
FT /note="Bifunctional protein FolD"
FT /id="PRO_0000268443"
FT BINDING 166..168
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01576"
FT BINDING 232
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01576"
FT HELIX 8..28
FT /evidence="ECO:0007829|PDB:4A5O"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:4A5O"
FT HELIX 45..60
FT /evidence="ECO:0007829|PDB:4A5O"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:4A5O"
FT HELIX 76..87
FT /evidence="ECO:0007829|PDB:4A5O"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:4A5O"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:4A5O"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:4A5O"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:4A5O"
FT HELIX 141..152
FT /evidence="ECO:0007829|PDB:4A5O"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:4A5O"
FT HELIX 172..181
FT /evidence="ECO:0007829|PDB:4A5O"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:4A5O"
FT HELIX 196..201
FT /evidence="ECO:0007829|PDB:4A5O"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:4A5O"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:4A5O"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:4A5O"
FT HELIX 246..252
FT /evidence="ECO:0007829|PDB:4A5O"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:4A5O"
FT HELIX 263..281
FT /evidence="ECO:0007829|PDB:4A5O"
SQ SEQUENCE 284 AA; 30549 MW; 22657CF7BEDE7967 CRC64;
MTAQLIDGKA IAANLRQQIA QRVTERRQQG LRVPGLAVIL VGTDPASQVY VAHKRKDCEE
VGFLSQAYDL PAETSQDDLL ALIDRLNDDP AIDGILVQLP LPAHLDASLL LERIHPDKDV
DGFHPYNIGR LAQRMPLLRP CTPKGIMTLL ASTGADLYGM DAVVVGASNI VGRPMALELL
LGGCTVTVTH RFTRDLADHV SRADLVVVAA GKPGLVKGEW IKEGAIVIDV GINRQADGRL
VGDVEYEVAA QRASWITPVP GGVGPMTRAC LLENTLHAAE HLHD
