ID Q79RA2_VIBCL Unreviewed; 165 AA.
AC Q79RA2;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 87.
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=dfrXII {ECO:0000313|EMBL:AAM52497.1};
GN Synonyms=dfrA12 {ECO:0000313|EMBL:ABV21787.1};
OS Vibrio cholerae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=666 {ECO:0000313|EMBL:AAM52497.1};
RN [1] {ECO:0000313|EMBL:AAM52497.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12183252; DOI=10.1128/AAC.46.9.2948-2955.2002;
RA Thungapathra M., Amita, Sinha K.K., Chaudhuri S.R., Garg P., Ramamurthy T.,
RA Nair G.B., Ghosh A.;
RT "Occurrence of antibiotic resistance gene cassettes aac(6')-Ib, dfrA5,
RT dfrA12, and ereA2 in class I integrons in non-O1, non-O139 Vibrio cholerae
RT strains in India.";
RL Antimicrob. Agents Chemother. 46:2948-2955(2002).
RN [2] {ECO:0000313|EMBL:ABV21787.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=9764 {ECO:0000313|EMBL:ABV21787.1};
RA Pan J.-C., Ye R., Meng D.-M.;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ABV21787.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=9764 {ECO:0000313|EMBL:ABV21787.1};
RX PubMed=18710912; DOI=10.1128/AAC.00375-08;
RA Pan J.C., Ye R., Wang H.Q., Xiang H.Q., Zhang W., Yu X.F., Meng D.M.,
RA He Z.S.;
RT "Vibrio cholerae O139 multiple-drug resistance mediated by Yersinia pestis
RT pIP1202-like conjugative plasmids.";
RL Antimicrob. Agents Chemother. 52:3829-3836(2008).
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|ARBA:ARBA00025067,
CC 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 ECO:0000256|RuleBase:RU004474}.
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DR EMBL; AY103459; AAM52497.1; -; Genomic_DNA.
DR EMBL; EU116440; ABV21787.1; -; Genomic_DNA.
DR RefSeq; WP_001083725.1; NZ_VMQH01000099.1.
DR AlphaFoldDB; Q79RA2; -.
DR SMR; Q79RA2; -.
DR GeneID; 84568342; -.
DR UniPathway; UPA00077; UER00158.
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; IPR017925; DHFR_CS.
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; PS00075; DHFR_1; 1.
DR PROSITE; PS51330; DHFR_2; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000194};
KW One-carbon metabolism {ECO:0000256|PIRNR:PIRNR000194};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000194}.
FT DOMAIN 7..162
FT /note="DHFR"
FT /evidence="ECO:0000259|PROSITE:PS51330"
SQ SEQUENCE 165 AA; 18127 MW; D264DED1377799C7 CRC64;
MNSESVRIYL VAAMGANRVI GNGPNIPWKI PGEQKIFRRL TEGKVVVMGR KTFESIGKPL
PNRHTLVISR QANYRATGCV VVSTLSHAIA LASELGNELY VAGGAEIYTL ALPHAHGVFL
SEVHQTFEGD AFFPMLNETE FELVSTETIQ AVIPYTHSVY ARRNG
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