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Database: UniProt
Entry: E6XMX2_SHEP2
LinkDB: E6XMX2_SHEP2
Original site: E6XMX2_SHEP2 
ID   E6XMX2_SHEP2            Unreviewed;       239 AA.
AC   E6XMX2;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Dihydromonapterin reductase {ECO:0000256|ARBA:ARBA00039631};
DE            EC=1.5.1.3 {ECO:0000256|ARBA:ARBA00012856};
DE            EC=1.5.1.50 {ECO:0000256|ARBA:ARBA00039145};
DE   AltName: Full=Dihydrofolate reductase {ECO:0000256|ARBA:ARBA00042299};
GN   OrderedLocusNames=Sput200_3351 {ECO:0000313|EMBL:ADV55740.1};
OS   Shewanella putrefaciens (strain 200).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=399804 {ECO:0000313|EMBL:ADV55740.1, ECO:0000313|Proteomes:UP000008209};
RN   [1] {ECO:0000313|EMBL:ADV55740.1, ECO:0000313|Proteomes:UP000008209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=200 {ECO:0000313|EMBL:ADV55740.1,
RC   ECO:0000313|Proteomes:UP000008209};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Kolker E., Lawrence C., McCue L.A., DiChristina T., Nealson K.,
RA   Fredrickson J.K., Woyke T.;
RT   "Complete sequence of Shewanella putrefaciens 200.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reduction of dihydromonapterin to
CC       tetrahydromonapterin. Also has lower activity with dihydrofolate.
CC       {ECO:0000256|ARBA:ARBA00037508}.
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|ARBA:ARBA00001315};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7,8-dihydromonapterin + H(+) + NADPH = 5,6,7,8-
CC         tetrahydromonapterin + NADP(+); Xref=Rhea:RHEA:34847,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:71175, ChEBI:CHEBI:71177; EC=1.5.1.50;
CC         Evidence={ECO:0000256|ARBA:ARBA00036516};
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. FolM subfamily. {ECO:0000256|ARBA:ARBA00038212}.
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DR   EMBL; CP002457; ADV55740.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6XMX2; -.
DR   KEGG; shp:Sput200_3351; -.
DR   PATRIC; fig|399804.5.peg.3470; -.
DR   HOGENOM; CLU_010194_1_3_6; -.
DR   OrthoDB; 9793499at2; -.
DR   Proteomes; UP000008209; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR43639:SF6; DIHYDROMONAPTERIN REDUCTASE; 1.
DR   PANTHER; PTHR43639; OXIDOREDUCTASE, SHORT-CHAIN DEHYDROGENASE/REDUCTASE FAMILY (AFU_ORTHOLOGUE AFUA_5G02870); 1.
DR   Pfam; PF13561; adh_short_C2; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563}.
SQ   SEQUENCE   239 AA;  26191 MW;  438B7C01FC3CF9DF CRC64;
     MTSPIIITGV GKRIGYALAK HLLAQGHSVI GTYRSHYPNI DKLRVLGATL IQCDFYDNVQ
     VQGLIDQLSQ YPKIRAIIHN ASDWLADSSQ TFTASEVIQR MMLVHVSVPY QLNLALASQL
     QAGAEEEIGA SDIIHITDYV AEKGSAKHIA YAASKAALHN LTLSFAAKFA PEVKVNSIAP
     AMILFNQGDD EAYQQKTLAK ALLPKEAGSE EIIDLVEYLL NSRYVTGRSH HVDGGRHLR
//
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