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Database: UniProt
Entry: A0A0N7GXL9_9GAMM
LinkDB: A0A0N7GXL9_9GAMM
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ID   A0A0N7GXL9_9GAMM        Unreviewed;       170 AA.
AC   A0A0N7GXL9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
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   ORFNames=AOY20_05760 {ECO:0000313|EMBL:ALH95083.1};
OS   Acinetobacter equi.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1324350 {ECO:0000313|EMBL:ALH95083.1, ECO:0000313|Proteomes:UP000064939};
RN   [1] {ECO:0000313|EMBL:ALH95083.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=114 {ECO:0000313|EMBL:ALH95083.1};
RX   PubMed=26620413;
RA   Poppel M.T., Skiebe E., Laue M., Bergmann H., Ebersberger I., Garn T.,
RA   Fruth A., Baumgardt S., Busse H.J., Wilharm G.;
RT   "Acinetobacter equi sp. nov. isolated from horse faeces.";
RL   Int. J. Syst. Evol. Microbiol. 0:0-0(2015).
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; CP012808; ALH95083.1; -; Genomic_DNA.
DR   RefSeq; WP_054580980.1; NZ_CP012808.1.
DR   AlphaFoldDB; A0A0N7GXL9; -.
DR   STRING; 1324350.AOY20_05760; -.
DR   KEGG; aei:AOY20_05760; -.
DR   OrthoDB; 9804315at2; -.
DR   UniPathway; UPA00077; UER00158.
DR   Proteomes; UP000064939; Chromosome.
DR   GO; GO:0004146; F:dihydrofolate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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:0016310; P:phosphorylation; 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   Kinase {ECO:0000313|EMBL:ALH95083.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000064939};
KW   Transferase {ECO:0000313|EMBL:ALH95083.1}.
FT   DOMAIN          7..170
FT                   /note="DHFR"
FT                   /evidence="ECO:0000259|PROSITE:PS51330"
SQ   SEQUENCE   170 AA;  19152 MW;  2C45A27CF6FFCB94 CRC64;
     MAFQNLEVVH VVAMDQKHCI GKGNDLPWHI SADLKHFKEI TQGGVVVMGR KTLESMGRTL
     PKRVNWIITR DLNWAFEGTK IAHSIDDALQ QAVTDVKASE KPDTIFIIGG GEIFKQTIDI
     ADRLELTHVE LDVQGDAHYP EIPNEFKKVA SEQHIDDKTG VAFEFATYRK
//
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