ID Q4JX60_CORJK Unreviewed; 234 AA.
AC Q4JX60;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 97.
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:CAI36597.1};
GN OrderedLocusNames=jk0440 {ECO:0000313|EMBL:CAI36597.1};
OS Corynebacterium jeikeium (strain K411).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=306537 {ECO:0000313|EMBL:CAI36597.1, ECO:0000313|Proteomes:UP000000545};
RN [1] {ECO:0000313|EMBL:CAI36597.1, ECO:0000313|Proteomes:UP000000545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K411 {ECO:0000313|EMBL:CAI36597.1,
RC ECO:0000313|Proteomes:UP000000545};
RX PubMed=15968079; DOI=10.1128/JB.187.13.4671-4682.2005;
RA Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT "Complete genome sequence and analysis of the multiresistant nosocomial
RT pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT human skin flora.";
RL J. Bacteriol. 187:4671-4682(2005).
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, ECO:0000256|RuleBase:RU004474}.
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DR EMBL; CR931997; CAI36597.1; -; Genomic_DNA.
DR RefSeq; WP_011273123.1; NC_007164.1.
DR AlphaFoldDB; Q4JX60; -.
DR STRING; 306537.jk0440; -.
DR GeneID; 3432572; -.
DR KEGG; cjk:jk0440; -.
DR PATRIC; fig|306537.10.peg.452; -.
DR eggNOG; COG0262; Bacteria.
DR HOGENOM; CLU_043966_5_0_11; -.
DR OrthoDB; 9804315at2; -.
DR UniPathway; UPA00077; UER00158.
DR Proteomes; UP000000545; Chromosome.
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 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};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CAI36597.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000545}.
FT DOMAIN 41..233
FT /note="DHFR"
FT /evidence="ECO:0000259|PROSITE:PS51330"
FT REGION 197..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 234 AA; 26096 MW; C5195C1E54449F60 CRC64;
MTPNNQPHRP TGYEPGDYPD LTAAAVSYAL EAKGISRDQV EIGMIWAQTT DGVIGDGADM
PWYLPEDLKH FKNATSGYPV VMGRTSWEAL DDGFRPLPDR TNYVITRQDN YDAPGGIVEP
SIPSALANAA EQILNELTDS ADKGEGADDR TPTVWVLGGG QVYAQCMPVA DRIVITEIDM
EAPERFQVYA PLVPEEEFEE SAQDWQESEK GHPVDQEVDT EQPLRYRFCT WTRR
//
