ID A0A132MXA1_9ACTN Unreviewed; 281 AA.
AC A0A132MXA1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Bifunctional protein FolD {ECO:0000256|HAMAP-Rule:MF_01576};
DE Includes:
DE RecName: Full=Methylenetetrahydrofolate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01576};
DE EC=1.5.1.5 {ECO:0000256|HAMAP-Rule:MF_01576};
DE Includes:
DE RecName: Full=Methenyltetrahydrofolate cyclohydrolase {ECO:0000256|HAMAP-Rule:MF_01576};
DE EC=3.5.4.9 {ECO:0000256|HAMAP-Rule:MF_01576};
GN Name=folD {ECO:0000256|HAMAP-Rule:MF_01576};
GN ORFNames=LI90_3581 {ECO:0000313|EMBL:KWX02538.1}, TH66_12425
GN {ECO:0000313|EMBL:KWX03636.1}, TR74_13030
GN {ECO:0000313|EMBL:KWX08857.1};
OS Carbonactinospora thermoautotrophica.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Carbonactinosporaceae; Carbonactinospora.
OX NCBI_TaxID=1469144 {ECO:0000313|EMBL:KWX02538.1, ECO:0000313|Proteomes:UP000070188};
RN [1] {ECO:0000313|EMBL:KWX03636.1, ECO:0000313|Proteomes:UP000070659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UBT1 {ECO:0000313|EMBL:KWX03636.1,
RC ECO:0000313|Proteomes:UP000070659};
RA MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA Prell J.;
RT "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT of multiple isolates of Streptomyces thermoautotrophicus.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000070598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UBT1 {ECO:0000313|Proteomes:UP000070598};
RA MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA Friesen M., Prell J.;
RT "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT of multiple isolates of Streptomyces thermoautotrophicus.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KWX02538.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H1 {ECO:0000313|EMBL:KWX02538.1};
RA MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA Woodward J., Friesen M., Prell J.;
RT "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT of multiple isolates of Streptomyces thermoautotrophicus.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000070188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H1 {ECO:0000313|Proteomes:UP000070188};
RA MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA Chang R., Ford T., Nguyen P.Q., Woodward J., Permingeat H., Joshi N.S.,
RA Silver P.A., Usadel B., Rutherford A.W., Friesen M., Prell J.;
RT "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT of multiple isolates of Streptomyces thermoautotrophicus.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01576}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methenyltetrahydrofolate + H2O = (6R)-10-
CC formyltetrahydrofolate + H(+); Xref=Rhea:RHEA:23700,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57455,
CC ChEBI:CHEBI:195366; EC=3.5.4.9; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01576};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-
CC 5,10-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:0000256|HAMAP-
CC Rule:MF_01576};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000256|ARBA:ARBA00004777, ECO:0000256|HAMAP-Rule:MF_01576}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01576}.
CC -!- SIMILARITY: Belongs to the tetrahydrofolate
CC dehydrogenase/cyclohydrolase family. {ECO:0000256|HAMAP-Rule:MF_01576}.
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:KWX02538.1}.
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DR EMBL; LAXD01000001; KWX02538.1; -; Genomic_DNA.
DR EMBL; JYIJ01000017; KWX03636.1; -; Genomic_DNA.
DR EMBL; JYIK01000929; KWX08857.1; -; Genomic_DNA.
DR RefSeq; WP_066889610.1; NZ_PQID01000001.1.
DR AlphaFoldDB; A0A132MXA1; -.
DR STRING; 1469144.LI90_3581; -.
DR PATRIC; fig|1469144.10.peg.3843; -.
DR OrthoDB; 9803580at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000070188; Unassembled WGS sequence.
DR Proteomes; UP000070598; Unassembled WGS sequence.
DR Proteomes; UP000070659; Unassembled WGS sequence.
DR GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniPathway.
DR CDD; cd01080; NAD_bind_m-THF_DH_Cyclohyd; 1.
DR Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_01576; THF_DHG_CYH; 1.
DR InterPro; IPR046346; Aminoacid_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; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom.
DR PANTHER; PTHR48099:SF5; C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR48099; C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC-RELATED; 1.
DR Pfam; PF00763; THF_DHG_CYH; 1.
DR Pfam; PF02882; THF_DHG_CYH_C; 1.
DR PRINTS; PR00085; THFDHDRGNASE.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01576};
KW Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01576};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01576};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP-
KW Rule:MF_01576};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_01576};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01576};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP-
KW Rule:MF_01576};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01576};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_01576}; Reference proteome {ECO:0000313|Proteomes:UP000070188}.
FT DOMAIN 6..120
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 123..280
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
FT BINDING 165..167
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01576"
FT BINDING 192
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01576"
FT BINDING 233
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01576"
SQ SEQUENCE 281 AA; 29299 MW; 4ECE59D48E5409E5 CRC64;
MTAQILDGKA TAAAIRDELR RRVAALRERG VAPGLGTVLV GDDPGSRSYV AGKHRDCAAV
GIASIQRELP ADATQAEVEA VVRELNEDPA CTGYIVQLPL PKGLDANRVL ELMDPAKDAD
GLHPTNLGRL VLGQPAPLPC TPRGIVELLR RYDVKIAGAE VVVIGRGVTV GRPLGLLLTR
RSENATVTLC HTGTKDLARH VRQADIVVAA AGVPGLVTAD MVKPGAVVLD VGITRTEAGL
VGDVDPRVRE VAGWVAPMPG GVGPMTRAML LTNVVEAAEA S
//
