ID A0A2M9HRF0_9BIFI Unreviewed; 220 AA.
AC A0A2M9HRF0;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=dihydrofolate reductase {ECO:0000256|ARBA:ARBA00012856};
DE EC=1.5.1.3 {ECO:0000256|ARBA:ARBA00012856};
GN ORFNames=CUU80_05085 {ECO:0000313|EMBL:PJM79396.1};
OS Bifidobacterium scaligerum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=2052656 {ECO:0000313|EMBL:PJM79396.1, ECO:0000313|Proteomes:UP000228755};
RN [1] {ECO:0000313|EMBL:PJM79396.1, ECO:0000313|Proteomes:UP000228755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TRED {ECO:0000313|Proteomes:UP000228755};
RA Mattarelli P., Modesto M., Bonetti A., Puglisi E., Morelli L.;
RT "Draft genome sequences of strains TRE 1, TRE D, TRE H and TRI 7, isolated
RT from tamarins, belonging to four potential novel Bifidobacterium species.";
RL Submitted (NOV-2017) 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, ECO:0000256|RuleBase:RU004474}.
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:PJM79396.1}.
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DR EMBL; PGLQ01000002; PJM79396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9HRF0; -.
DR OrthoDB; 9804315at2; -.
DR UniPathway; UPA00077; UER00158.
DR Proteomes; UP000228755; Unassembled WGS sequence.
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 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:PJM79396.1}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000228755};
KW Transferase {ECO:0000313|EMBL:PJM79396.1}.
FT DOMAIN 36..220
FT /note="DHFR"
FT /evidence="ECO:0000259|PROSITE:PS51330"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 220 AA; 24451 MW; 6B32E7424598CED3 CRC64;
MEHDSSRSGY HEPEPGTAGL EVTEEDWGDD FPKTFSVNLI WAEARDKEGR AGAIGLKGGM
PWHLSEDMKH FKELTVSHPV IMGRKTWESL DMKYRPLPNR DNIVVSHDPM YRAPGATVVT
SLEDALDLAR QEAIPDDGLD RSEIWIIGGA QLFAEALPFA DKAYVTMLAA NVEADTYAPD
MHALVESGLW QESEVGAWHT PANPKSGIDS YRFVLLTKTK
//
