(data stored in ACNUC7421 zone)

SWISSPROT: Q4ZZ93_PSEU2

ID   Q4ZZ93_PSEU2            Unreviewed;       281 AA.
AC   Q4ZZ93;
DT   07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 97.
DE   RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862};
DE            EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862};
GN   OrderedLocusNames=Psyr_0459 {ECO:0000313|EMBL:AAY35529.1};
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918 {ECO:0000313|EMBL:AAY35529.1, ECO:0000313|Proteomes:UP000000426};
RN   [1] {ECO:0000313|EMBL:AAY35529.1, ECO:0000313|Proteomes:UP000000426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a {ECO:0000313|EMBL:AAY35529.1,
RC   ECO:0000313|Proteomes:UP000000426};
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + NAD(+) = (6R)-
CC         5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH;
CC         Xref=Rhea:RHEA:19821, ChEBI:CHEBI:15378, ChEBI:CHEBI:15636,
CC         ChEBI:CHEBI:18608, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.5.1.20; Evidence={ECO:0000256|RuleBase:RU003862};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU003862};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000256|RuleBase:RU003862}.
CC   -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase
CC       family. {ECO:0000256|RuleBase:RU003862}.
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DR   EMBL; CP000075; AAY35529.1; -; Genomic_DNA.
DR   RefSeq; WP_003346344.1; NC_007005.1.
DR   RefSeq; YP_233567.1; NC_007005.1.
DR   STRING; 205918.Psyr_0459; -.
DR   EnsemblBacteria; AAY35529; AAY35529; Psyr_0459.
DR   GeneID; 3365935; -.
DR   KEGG; psb:Psyr_0459; -.
DR   PATRIC; fig|205918.7.peg.477; -.
DR   eggNOG; ENOG4105SYT; Bacteria.
DR   eggNOG; COG0685; LUCA.
DR   HOGENOM; HOG000246232; -.
DR   KO; K00297; -.
DR   OMA; FIRAETG; -.
DR   BioCyc; PSYR205918:G1G4J-460-MONOMER; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000000426; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:InterPro.
DR   GO; GO:0004489; F:methylenetetrahydrofolate reductase (NAD(P)H) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR   CDD; cd00537; MTHFR; 1.
DR   InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR   InterPro; IPR003171; Mehydrof_redctse.
DR   InterPro; IPR004620; MTHF_reductase_bac.
DR   Pfam; PF02219; MTHFR; 1.
DR   SUPFAM; SSF51730; SSF51730; 1.
DR   TIGRFAMs; TIGR00676; fadh2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4ZZ93.
DR   SWISS-2DPAGE; Q4ZZ93.
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004255};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000426};
KW   FAD {ECO:0000256|RuleBase:RU003862};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003862};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003862}.
SQ   SEQUENCE   281 AA;  31398 MW;  276FE887DF746029 CRC64;
     MSQERRFSFE FFPTKTDAGH EKLLTVARQL ATYNPDFFSC TYGAGGSTRD RTLNTVLQLE
     NEIKVPAAPH LSCVGDSKDD LRNLLAQYKD AGIKRIVALR GDLPSGMGMA SGELRHANDL
     VSFIRQESGS HFHIEVAAYP EMHPQARNFE DDLKHFVNKA NAGADSAITQ YFFNADSYFN
     FVERVEKMGV SIPIVPGIMP ITNYSKLARF SDACGAEIPR WIRKQLEAYG DDVQSIQAFG
     EEVITQMCER LLQGGAPGLH FYTLNQAEPS LAVWNNLQLP R
//

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