ID H2TGW3_TAKRU Unreviewed; 757 AA.
AC H2TGW3;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Methionine synthase reductase {ECO:0000256|ARBA:ARBA00040659};
DE EC=1.16.1.8 {ECO:0000256|ARBA:ARBA00039088};
GN Name=MTRR {ECO:0000313|Ensembl:ENSTRUP00000023912.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000023912.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000023912.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000023912.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR RefSeq; XP_011606110.1; XM_011607808.1.
DR AlphaFoldDB; H2TGW3; -.
DR Ensembl; ENSTRUT00000024011.3; ENSTRUP00000023912.3; ENSTRUG00000009518.3.
DR GeneID; 101070210; -.
DR CTD; 4552; -.
DR GeneTree; ENSGT00940000155822; -.
DR OrthoDB; 276396at2759; -.
DR Proteomes; UP000005226; Chromosome 10.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd06203; methionine_synthase_red; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 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 PANTHER; PTHR19384:SF84; METHIONINE SYNTHASE REDUCTASE; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
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; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226}.
FT DOMAIN 33..176
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 323..584
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 191..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 757 AA; 83801 MW; 254B91B8BBF8795A CRC64;
MAFRSVRASL LQSNIYLLPH ALCSMPSEMK PRFVLLYGSQ KGQAQAIAEG VAEEAETHGL
FAELSCLENN EKYNLETETA PVVFIVSTTG DGEPPDNALK FVRNIKKKTL SSDHYKHISY
ALLGLGDTNY ANFCNCGKAI DRRLRELGAS QFYASGYADD GVGLELVVDP WIKGLWNAIK
EELSNMTSKQ TECVKEEVRD SSKETPDPST ADMQLNLLSI ANCQNCKSIG QSEKLANLAS
PSVSTTQTAG SDLRPDSSSR RIGLSSRTDG ALSADAGVAS LTHSLPPLSQ SALNIPALPP
PYLCVSLQEM ETTEDIFGPL NKENLQEVPI SKATQLTRGD SVKTALLLEL DISTLPAMTY
QPGDAFDVYW PNSATEVEDM LHRLGLQDQR NHRVLISLLK DTKKRGAQVP SYIPQNASLL
YLLTWCLEIR SVPKKAFLRA LVEYTVDGVQ KRRLQELCSK QGTTDYNSHL REQSLSILEL
LNAFPSCSPP LSILIEHVPK LQPRPYSVAS SCLRHPGKLN FVFNIVEFPA CSGRTAGRRG
LCTGGLFDLI SSRLVLPGNV KSSSKPALPK IHVNLRPTCT FRPPADVSVP FMMVGPGTGV
APFIGFLQQR EEQRRQNPLA TFGETWLFFG CRHRDQDFLF REELESFVSS GVLSHLQLSF
SRDDPEEQEG ADETISPTAQ RRYVQHNLKL HGRQVTDILL KQKGCIYVCG DARNMAKDVD
TTLMEVIKAE LGMDQLEAMK TLAALREEKR YLQDIWG
//
