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Database: UniProt
Entry: D3AQZ1_9CLOT
LinkDB: D3AQZ1_9CLOT
Original site: D3AQZ1_9CLOT 
ID   D3AQZ1_9CLOT            Unreviewed;       178 AA.
AC   D3AQZ1;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Dihydrofolate reductase {ECO:0000256|ARBA:ARBA00012856, ECO:0000256|PIRNR:PIRNR000194};
DE            EC=1.5.1.3 {ECO:0000256|ARBA:ARBA00012856, ECO:0000256|PIRNR:PIRNR000194};
GN   Name=folA {ECO:0000313|EMBL:EFC95769.1};
GN   ORFNames=CLOSTHATH_06047 {ECO:0000313|EMBL:EFC95769.1};
OS   Hungatella hathewayi DSM 13479.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hungatella.
OX   NCBI_TaxID=566550 {ECO:0000313|EMBL:EFC95769.1, ECO:0000313|Proteomes:UP000004968};
RN   [1] {ECO:0000313|EMBL:EFC95769.1, ECO:0000313|Proteomes:UP000004968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13479 {ECO:0000313|EMBL:EFC95769.1,
RC   ECO:0000313|Proteomes:UP000004968};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential
CC       reaction for de novo glycine and purine synthesis, and for DNA
CC       precursor synthesis. {ECO:0000256|PIRNR:PIRNR000194}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate +
CC         H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.5.1.3;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000194};
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-
CC       tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004903, ECO:0000256|PIRNR:PIRNR000194}.
CC   -!- SIMILARITY: Belongs to the dihydrofolate reductase family.
CC       {ECO:0000256|ARBA:ARBA00009539, ECO:0000256|PIRNR:PIRNR000194}.
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:EFC95769.1}.
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DR   EMBL; ACIO01000679; EFC95769.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3AQZ1; -.
DR   HOGENOM; CLU_043966_5_2_9; -.
DR   UniPathway; UPA00077; UER00158.
DR   Proteomes; UP000004968; Unassembled WGS sequence.
DR   GO; GO:0004146; F:dihydrofolate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006545; P:glycine biosynthetic process; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00209; DHFR; 1.
DR   Gene3D; 3.40.430.10; Dihydrofolate Reductase, subunit A; 1.
DR   InterPro; IPR012259; DHFR.
DR   InterPro; IPR024072; DHFR-like_dom_sf.
DR   InterPro; IPR001796; DHFR_dom.
DR   PANTHER; PTHR48069; DIHYDROFOLATE REDUCTASE; 1.
DR   PANTHER; PTHR48069:SF3; DIHYDROFOLATE REDUCTASE; 1.
DR   Pfam; PF00186; DHFR_1; 1.
DR   PIRSF; PIRSF000194; DHFR; 1.
DR   PRINTS; PR00070; DHFR.
DR   SUPFAM; SSF53597; Dihydrofolate reductase-like; 1.
DR   PROSITE; PS51330; DHFR_2; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|PIRNR:PIRNR000194};
KW   One-carbon metabolism {ECO:0000256|PIRNR:PIRNR000194};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000194,
KW   ECO:0000313|EMBL:EFC95769.1}.
FT   DOMAIN          11..172
FT                   /note="DHFR"
FT                   /evidence="ECO:0000259|PROSITE:PS51330"
SQ   SEQUENCE   178 AA;  20462 MW;  123D5B9224738B74 CRC64;
     MKFRNRTGGN YMKAIVAVDE AWGIGKDGKL LTHLPEDMKF FRTVTKGKVV VMGRKTLQSF
     PDAKPLKNRI NIVLTSDAAL NGEGLIVCRS VADALRQLKE YDSDDVYIIG GQSVYEQFLP
     YCDTAYVTRM KRDFGADTWF VNLDRQEGWE ETETGDEKEY EGLHFTFCTY KNRNCQDW
//
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