MTRR_CAEEL
ID MTRR_CAEEL Reviewed; 682 AA.
AC Q17574; Q8I4N2;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Methionine synthase reductase {ECO:0000312|WormBase:C01G6.6a};
DE Short=MSR;
DE EC=1.16.1.8 {ECO:0000250|UniProtKB:Q9UBK8};
GN Name=mtrr-1 {ECO:0000312|WormBase:C01G6.6a};
GN Synonyms=tag-165 {ECO:0000312|WormBase:C01G6.6a};
GN ORFNames=C01G6.6 {ECO:0000312|WormBase:C01G6.6a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Involved in the reductive regeneration of cob(I)alamin
CC cofactor required for the maintenance of methionine synthase in a
CC functional state. {ECO:0000250|UniProtKB:Q9UBK8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + 2 methylcob(III)alamin-[methionine synthase] + NADP(+)
CC + 2 S-adenosyl-L-homocysteine = 2 cob(II)alamin-[methionine synthase]
CC + NADPH + 2 S-adenosyl-L-methionine; Xref=Rhea:RHEA:23908, Rhea:RHEA-
CC COMP:14714, Rhea:RHEA-COMP:14715, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16304, ChEBI:CHEBI:28115, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:58349, ChEBI:CHEBI:59789; EC=1.16.1.8;
CC Evidence={ECO:0000250|UniProtKB:Q9UBK8};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q9UBK8};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q9UBK8};
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DR EMBL; BX284602; CAA84637.1; -; Genomic_DNA.
DR PIR; T18838; T18838.
DR RefSeq; NP_495978.1; NM_063577.4.
DR AlphaFoldDB; Q17574; -.
DR SMR; Q17574; -.
DR BioGRID; 39795; 3.
DR STRING; 6239.C01G6.6a.2; -.
DR iPTMnet; Q17574; -.
DR EPD; Q17574; -.
DR PaxDb; Q17574; -.
DR PeptideAtlas; Q17574; -.
DR EnsemblMetazoa; C01G6.6a.1; C01G6.6a.1; WBGene00006510.
DR GeneID; 174471; -.
DR KEGG; cel:CELE_C01G6.6; -.
DR UCSC; C01G6.6b.1; c. elegans.
DR CTD; 174471; -.
DR WormBase; C01G6.6a; CE00868; WBGene00006510; mtrr-1.
DR eggNOG; KOG1158; Eukaryota.
DR GeneTree; ENSGT00940000155822; -.
DR HOGENOM; CLU_001570_17_7_1; -.
DR InParanoid; Q17574; -.
DR OMA; TDRREHC; -.
DR OrthoDB; 318396at2759; -.
DR PhylomeDB; Q17574; -.
DR Reactome; R-CEL-156581; Methylation.
DR Reactome; R-CEL-1614635; Sulfur amino acid metabolism.
DR Reactome; R-CEL-9759218; Cobalamin (Cbl) metabolism.
DR PRO; PR:Q17574; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00006510; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030586; F:[methionine synthase] reductase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0050667; P:homocysteine metabolic process; IBA:GO_Central.
DR GO; GO:0009086; P:methionine biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.20.990.10; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52218; SSF52218; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; FAD; Flavoprotein; FMN; Methionine biosynthesis;
KW NADP; Oxidoreductase; Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..682
FT /note="Methionine synthase reductase"
FT /id="PRO_0000096638"
FT DOMAIN 4..147
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT DOMAIN 271..516
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 93..124
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 293
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9UBK8"
FT BINDING 455..458
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9UBK8"
FT BINDING 488..491
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9UBK8"
FT BINDING 607..609
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9UBK8"
FT BINDING 643
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9UBK8"
FT BINDING 681
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9UBK8"
SQ SEQUENCE 682 AA; 76834 MW; C7E6D9AA07C1D2FD CRC64;
MTDFLIAFGS QTGQAETIAK SLKEKAELIG LTPRLHALDE NEKKFNLNEE KLCAIVVSST
GDGDAPDNCA RFVRRINRNS LENEYLKNLD YVLLGLGDSN YSSYQTIPRK IDKQLTALGA
NRLFDRAEAD DQVGLELEVE PWIEKFFATL ASRFDISADK MNAITESSNL KLNQVKTEEE
KKALLQKRIE DEESDDEGRG RVIGIDMLIP EHYDYPEISL LKGSQTLSND ENLRVPIAPQ
PFIVSSVSNR KLPEDTKLEW QNLCKMPGVV TKPFEVLVVS AEFVTDPFSK KIKTKRMITV
DFGDHAAELQ YEPGDAIYFC VPNPALEVNF ILKRCGVLDI ADQQCELSIN PKTEKINAQI
PGHVHKITTL RHMFTTCLDI RRAPGRPLIR VLAESTSDPN EKRRLLELCS AQGMKDFTDF
VRTPGLSLAD MLFAFPNVKP PVDRLIELLP RLIPRPYSMS SYENRKARLI YSEMEFPATD
GRRHSRKGLA TDWLNSLRIG DKVQVLGKEP ARFRLPPLGM TKNSAGKLPL LMVGPGTGVS
VFLSFLHFLR KLKQDSPSDF VDVPRVLFFG CRDSSVDAIY MSELEMFVSE GILTDLIICE
SEQKGERVQD GLRKYLDKVL PFLTASTESK IFICGDAKGM SKDVWQCFSD IVASDQGIPD
LEAKKKLMDL KKSDQYIEDV WG
