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Bifunctional protein FolD [Includes: Methylenetetrahydrofolate dehydrogenase (EC 1.5.1.5); Methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9)]

 F7XW23_MIDMI            Unreviewed;       292 AA.
F7XW23;
21-SEP-2011, integrated into UniProtKB/TrEMBL.
21-SEP-2011, sequence version 1.
30-AUG-2017, entry version 45.
RecName: Full=Bifunctional protein FolD {ECO:0000256|HAMAP-Rule:MF_01576};
Includes:
RecName: Full=Methenyltetrahydrofolate cyclohydrolase {ECO:0000256|HAMAP-Rule:MF_01576};
EC=3.5.4.9 {ECO:0000256|HAMAP-Rule:MF_01576};
Includes:
RecName: Full=Methylenetetrahydrofolate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01576};
EC=1.5.1.5 {ECO:0000256|HAMAP-Rule:MF_01576};
Name=folD {ECO:0000256|HAMAP-Rule:MF_01576,
ECO:0000313|EMBL:AEI88872.1};
OrderedLocusNames=midi_00572 {ECO:0000313|EMBL:AEI88872.1};
Midichloria mitochondrii (strain IricVA).
Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
Candidatus Midichloriaceae; Candidatus Midichloria.
NCBI_TaxID=696127 {ECO:0000313|EMBL:AEI88872.1, ECO:0000313|Proteomes:UP000006639};
[1] {ECO:0000313|EMBL:AEI88872.1, ECO:0000313|Proteomes:UP000006639}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IricVA {ECO:0000313|EMBL:AEI88872.1,
ECO:0000313|Proteomes:UP000006639};
PubMed=21690562; DOI=10.1093/molbev/msr159;
Sassera D., Lo N., Epis S., D'Auria G., Montagna M., Comandatore F.,
Horner D., Pereto J., Luciano A.M., Franciosi F., Ferri E., Crotti E.,
Bazzocchi C., Daffonchio D., Sacchi L., Moya A., Latorre A., Bandi C.;
"Phylogenomic evidence for the presence of a flagellum and cbb3
oxidase in the free-living mitochondrial ancestor.";
Mol. Biol. Evol. 28:3285-3296(2011).
-!- FUNCTION: Catalyzes the oxidation of 5,10-
methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and
then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-
formyltetrahydrofolate. {ECO:0000256|HAMAP-Rule:MF_01576,
ECO:0000256|SAAS:SAAS00730939}.
-!- CATALYTIC ACTIVITY: 5,10-methenyltetrahydrofolate + H(2)O = 10-
formyltetrahydrofolate. {ECO:0000256|HAMAP-Rule:MF_01576,
ECO:0000256|SAAS:SAAS00020423}.
-!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + NADP(+) =
5,10-methenyltetrahydrofolate + NADPH. {ECO:0000256|HAMAP-
Rule:MF_01576, ECO:0000256|SAAS:SAAS00730961}.
-!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
{ECO:0000256|HAMAP-Rule:MF_01576, ECO:0000256|SAAS:SAAS00730924}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01576,
ECO:0000256|SAAS:SAAS00730963}.
-!- SIMILARITY: Belongs to the tetrahydrofolate
dehydrogenase/cyclohydrolase family. {ECO:0000256|HAMAP-
Rule:MF_01576, ECO:0000256|SAAS:SAAS00730920}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01576}.
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EMBL; CP002130; AEI88872.1; -; Genomic_DNA.
RefSeq; WP_013951084.1; NC_015722.1.
STRING; 696127.midi_00572; -.
EnsemblBacteria; AEI88872; AEI88872; midi_00572.
KEGG; mmn:midi_00572; -.
eggNOG; ENOG4105CN0; Bacteria.
eggNOG; COG0190; LUCA.
KO; K01491; -.
OMA; AGKLCGD; -.
OrthoDB; POG091H0041; -.
UniPathway; UPA00193; -.
Proteomes; UP000006639; Chromosome.
GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; IEA:UniProtKB-HAMAP.
GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:UniProtKB-HAMAP.
GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
HAMAP; MF_01576; THF_DHG_CYH; 1.
InterPro; IPR016040; NAD(P)-bd_dom.
InterPro; IPR000672; THF_DH/CycHdrlase.
InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom.
InterPro; IPR020867; THF_DH/CycHdrlase_CS.
InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom.
PANTHER; PTHR10025; PTHR10025; 1.
Pfam; PF00763; THF_DHG_CYH; 1.
Pfam; PF02882; THF_DHG_CYH_C; 1.
PRINTS; PR00085; THFDHDRGNASE.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00766; THF_DHG_CYH_1; 1.
PROSITE; PS00767; THF_DHG_CYH_2; 1.
3: Inferred from homology;
Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01576,
ECO:0000256|SAAS:SAAS00730931, ECO:0000256|SAAS:SAAS00730933};
Complete proteome {ECO:0000313|Proteomes:UP000006639};
Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01576,
ECO:0000256|SAAS:SAAS00730933};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_01576,
ECO:0000256|SAAS:SAAS00020439};
Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01576,
ECO:0000256|SAAS:SAAS00730931};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01576,
ECO:0000256|SAAS:SAAS00020419};
NADP {ECO:0000256|HAMAP-Rule:MF_01576, ECO:0000256|SAAS:SAAS00730866};
One-carbon metabolism {ECO:0000256|HAMAP-Rule:MF_01576,
ECO:0000256|SAAS:SAAS00020466};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01576,
ECO:0000256|SAAS:SAAS00020431, ECO:0000313|EMBL:AEI88872.1};
Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01576,
ECO:0000256|SAAS:SAAS00730882};
Reference proteome {ECO:0000313|Proteomes:UP000006639}.
DOMAIN 6 126 THF_DHG_CYH. {ECO:0000259|Pfam:PF00763}.
DOMAIN 130 287 THF_DHG_CYH_C.
{ECO:0000259|Pfam:PF02882}.
NP_BIND 172 174 NADP. {ECO:0000256|HAMAP-Rule:MF_01576}.
BINDING 197 197 NADP. {ECO:0000256|HAMAP-Rule:MF_01576}.
BINDING 238 238 NADP; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01576}.
SEQUENCE 292 AA; 31903 MW; CF936D7D90E79E4E CRC64;
MQNCEIIDGK LYAAEVLERV KSKIGHLSTV ICKTQRATLG LAVILVGTDA ASQIYVNNKA
KKAKEIGFNS EVYKFPQTAT EQEIIECIER LNSDPNVNGI LVQLPLPQHI NTQKIIDTVN
YEKDVDGFST YNVGLLNSWQ DSLEPCTPQG VLILLHEILG TNISGKKAVI LGRSRIVGRP
MASILIRKGC SVTSLNSNSY NIKDECRTAD ILISAVGSPS FIKGDWIKKG ACVIDVGIVK
VNDKLYGDVD FESVRKVAGF LTPVPGGVGP MTVSCLMLNT IKAAYKQYDI KW


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