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Database: UniProt
Entry: E7FUD6_ERYRH
LinkDB: E7FUD6_ERYRH
Original site: E7FUD6_ERYRH 
ID   E7FUD6_ERYRH            Unreviewed;       150 AA.
AC   E7FUD6;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=dihydrofolate reductase {ECO:0000256|ARBA:ARBA00012856};
DE            EC=1.5.1.3 {ECO:0000256|ARBA:ARBA00012856};
GN   Name=folA {ECO:0000313|EMBL:EFY09739.1};
GN   ORFNames=HMPREF0357_10534 {ECO:0000313|EMBL:EFY09739.1};
OS   Erysipelothrix rhusiopathiae ATCC 19414.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Erysipelothrix.
OX   NCBI_TaxID=525280 {ECO:0000313|EMBL:EFY09739.1, ECO:0000313|Proteomes:UP000003028};
RN   [1] {ECO:0000313|EMBL:EFY09739.1, ECO:0000313|Proteomes:UP000003028}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19414 {ECO:0000313|EMBL:EFY09739.1,
RC   ECO:0000313|Proteomes:UP000003028};
RA   Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA   Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA   Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA   Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA   Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA   Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA   Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA   Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA   Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA   Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA   Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA   Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA   Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA   Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA   Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-
CC       tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004903}.
CC   -!- SIMILARITY: Belongs to the dihydrofolate reductase family.
CC       {ECO:0000256|ARBA:ARBA00009539}.
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:EFY09739.1}.
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DR   EMBL; ACLK02000001; EFY09739.1; -; Genomic_DNA.
DR   RefSeq; WP_003773894.1; NZ_ACLK02000001.1.
DR   AlphaFoldDB; E7FUD6; -.
DR   STRING; 1648.A2I91_04540; -.
DR   GeneID; 60953426; -.
DR   OrthoDB; 9804315at2; -.
DR   UniPathway; UPA00077; UER00158.
DR   Proteomes; UP000003028; 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   PRINTS; PR00070; DHFR.
DR   SUPFAM; SSF53597; Dihydrofolate reductase-like; 1.
DR   PROSITE; PS51330; DHFR_2; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000313|EMBL:EFY09739.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003028}.
FT   DOMAIN          1..150
FT                   /note="DHFR"
FT                   /evidence="ECO:0000259|PROSITE:PS51330"
SQ   SEQUENCE   150 AA;  17351 MW;  F10203DF5769611D CRC64;
     MIKIIVAMNN HRTIGLNGSM PWHNKEDLQH FRKSTLNQKV VMGRKTFEGL PKKLDNREIY
     VVTRNASIEN AIPDLRAFLM QHKESSEDIF IAGGGEIYAQ SLPFAHELII SYIPNDVIGD
     TFFPDFSDLE FKIKNQVEYS TFKQVTYERI
//
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