ID G2EDM6_9FLAO Unreviewed; 300 AA.
AC G2EDM6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=dihydrofolate reductase {ECO:0000256|ARBA:ARBA00012856};
DE EC=1.5.1.3 {ECO:0000256|ARBA:ARBA00012856};
GN ORFNames=BZARG_1377 {ECO:0000313|EMBL:EGV43549.1};
OS Bizionia argentinensis JUB59.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Bizionia.
OX NCBI_TaxID=1046627 {ECO:0000313|EMBL:EGV43549.1, ECO:0000313|Proteomes:UP000003730};
RN [1] {ECO:0000313|EMBL:EGV43549.1, ECO:0000313|Proteomes:UP000003730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JUB59 {ECO:0000313|EMBL:EGV43549.1,
RC ECO:0000313|Proteomes:UP000003730};
RX PubMed=18842857; DOI=10.1099/ijs.0.65599-0;
RA Bercovich A., Vazquez S.C., Yankilevich P., Coria S.H., Foti M.,
RA Hernandez E., Vidal A., Ruberto L., Melo C., Marenssi S., Criscuolo M.,
RA Memoli M., Arguelles M., Mac Cormack W.P.;
RT "Bizionia argentinensis sp. nov., isolated from surface marine water in
RT Antarctica.";
RL Int. J. Syst. Evol. Microbiol. 58:2363-2367(2008).
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:EGV43549.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFXZ01000025; EGV43549.1; -; Genomic_DNA.
DR RefSeq; WP_008637204.1; NZ_AFXZ01000025.1.
DR AlphaFoldDB; G2EDM6; -.
DR STRING; 1046627.BZARG_1377; -.
DR PATRIC; fig|1046627.3.peg.1624; -.
DR eggNOG; COG0262; Bacteria.
DR OrthoDB; 9804315at2; -.
DR UniPathway; UPA00077; UER00158.
DR Proteomes; UP000003730; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR025698; 2TM_dom.
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; PF13239; 2TM; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000003730};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 33..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 140..299
FT /note="DHFR"
FT /evidence="ECO:0000259|PROSITE:PS51330"
SQ SEQUENCE 300 AA; 34991 MW; 3DD351BA6601AA35 CRC64;
MFGKKKESTT EIDKEQLELI KTAQKRIKQK KRLYAHFVIF LIGAVFLILA NTVLGIGQTF
RPFDIDWFVF AIAIWLFIFI YHLFSVFITS KLLSKKWEEK QLNQIVAKQK KRIAELKDQV
EQDIPLPERK SLRAPSRKSD ITIIVAAGEN NSIGKDNQLI WHLSDDLKRF KNLTNGHHII
MGRKTFETFK KPLPNRKHVV ITRQDNYQVP EGVIVVNNLA DALDASRTDK QPFIIGGGEI
YKQAMDFADK LEITRVHAEF EADTFFPEID MANWKEVTKT QHQKDENHAY DFSFITYIRH
//
