ID A0A0D2N4U9_9CHLO Unreviewed; 1561 AA.
AC A0A0D2N4U9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Methionine synthase reductase {ECO:0000256|ARBA:ARBA00040659};
DE EC=1.16.1.8 {ECO:0000256|ARBA:ARBA00039088};
GN ORFNames=MNEG_0613 {ECO:0000313|EMBL:KIZ07342.1};
OS Monoraphidium neglectum.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Selenastraceae; Monoraphidium.
OX NCBI_TaxID=145388 {ECO:0000313|EMBL:KIZ07342.1, ECO:0000313|Proteomes:UP000054498};
RN [1] {ECO:0000313|EMBL:KIZ07342.1, ECO:0000313|Proteomes:UP000054498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 48.87 {ECO:0000313|EMBL:KIZ07342.1,
RC ECO:0000313|Proteomes:UP000054498};
RX PubMed=24373495; DOI=10.1186/1471-2164-14-926;
RA Bogen C., Al-Dilaimi A., Albersmeier A., Wichmann J., Grundmann M.,
RA Rupp O., Lauersen K.J., Blifernez-Klassen O., Kalinowski J., Goesmann A.,
RA Mussgnug J.H., Kruse O.;
RT "Reconstruction of the lipid metabolism for the microalga Monoraphidium
RT neglectum from its genome sequence reveals characteristics suitable for
RT biofuel production.";
RL BMC Genomics 14:926-926(2013).
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 EMBL; KK100271; KIZ07342.1; -; Genomic_DNA.
DR RefSeq; XP_013906361.1; XM_014050907.1.
DR STRING; 145388.A0A0D2N4U9; -.
DR GeneID; 25726731; -.
DR KEGG; mng:MNEG_0613; -.
DR OrthoDB; 315840at2759; -.
DR Proteomes; UP000054498; Unassembled WGS sequence.
DR GO; GO:0030586; F:[methionine synthase] reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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 Coiled coil {ECO:0000256|SAM:Coils}; 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 Methyltransferase {ECO:0000313|EMBL:KIZ07342.1};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KIZ07342.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054498};
KW Transferase {ECO:0000313|EMBL:KIZ07342.1}.
FT DOMAIN 695..840
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 1140..1393
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 106..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 20..47
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 212..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1008
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1067
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1561 AA; 161589 MW; 9954D7118AAF2A0E CRC64;
MARDGSPRAA EEAAWLRRML EKEQQARATA EQALAAERLR NALLEREAAQ DMGDSLCMYL
SNSRDPATAS LDAEGGGTQL PFPAASPGNW SVYSTKGLGL DRPLAAADDS ARTPPAGRDQ
RSRLGGGGAG AHAAEFATPQ RPLPCDEAAE DATSVGGRGG QGRLHQQIVE MSTRLKGFAS
EWVQRLEAME ERPREGIASD ARQAPPEVPQ DAAQQPATTG QRPQQRPLET PVVPAQTRRD
GVVAEEPLAC AEGSPLEAWC AQQQQRRPQL NAQRQQRAQP TPSASDESGA DGRVEVGLAL
VTCDDAACFQ DACPSFGDDS RGGPAHDPWH HQIPGGGAEL DRYTGSSGDH DHGFVDAQPP
SPAHSAASGP LSAARGALSC RLAARAGRAQ PHPHAAAAAA ATGVTAPAAP PSQAAPHGWA
GADGNVSKSF SHASNGSGAA QEEAGLRSSI TSPLMDPDVD LAPPRKSGMS RAGTRPLGDV
SRAGGAPAAQ QRAAAAAAAA PPDFESSDDD DYYEDPTKST VTMTVGAAGR AAGKGAAAAQ
VAAPALQQVA GDRRTTAEAA AEHFAAAERA TAARAARRTD SGAKDRQHAL NEALKLLHSE
FAEPAAPMAA AAGTEGGSAE QQQQQQEQKQ QQAAGAAASP PQASRRSSSA AAGDTHTLPE
AAPAAATATL PPPTAPAWSV SVTPHNTAAR PQPRAVFLYA SQTGNGREIA RTLQTEAGRR
GVPADVMALD ELGFPSFGAS KTPVAVIVTS STGDGEPPDN GAAFFKQLLA PAQAKGWRLE
GVKFALLGLG DSSYSRFMAA PRAMRARLVE LGAEEFYAAG EADDSEGMDK TVEPWCENLW
APLKTALLDA SGGPGGGGAA VAAHALAGTL AAEGGPALAA AHAPLAAAPR LAAEASKGSA
AQAAAAVAAV PKVYLEISMM SLGDSADLGE LEPPSRAEGG GSGSRPGSGP QQQQHLSHLA
PTVAGVQLRG SEREAAEEGA PQGQPLEEER QQAQEARSDA KPQQELSAED TEEQQQEEEQ
QQQQQQQQEE EQQQRDEEQE EERSQQEGDD QAPQEEGPQQ AQPQAGQPVQ AAPREPGGLV
GGLAPEGADL KGAPGLAPPR VEVSFDVAPA VSEDVRAREL SWPSEEQRKF RKPTGAYSAA
APFYARVAEA RLLTAPGSDR VVVHCELDIA GSGITHKAGD ALAVLPQNDP EMVAALLQRL
GLDGERVFEI KAAGRPAPGA TLLPHIVSPC SLRHALTHNV DIAGKPQKGL LRLLAEHCRN
EAEKRTLLFL CAKAGAADYT REIVAGHPCL LDLLNRFASC APPLAALLDA LPPLAPRAYA
ISAAPAAGAG ASAARLQFAF RAVSFQAPSG RCAGVATGWL QRLLAPRLAG EGTADADAWM
PILLRPSQTF APPPQLATPL IMIGSGTGTT PFRAFLQERA AARAAAAAGT AAAAAAPAVG
EAWLYAGCRR RDEDFLYGAD FDAFEASGDL TRLRVACSRE GDKRAYVQHL VRQDGAALAD
LIVRRGARVC VCGEGLGMAR EVHAALAAVL HAHVGMSEGE ANEELRAMAE AGAYVREASS
P
//
