ID A0A087SBA2_AUXPR Unreviewed; 622 AA.
AC A0A087SBA2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Methionine synthase reductase {ECO:0000256|ARBA:ARBA00040659};
DE EC=1.16.1.8 {ECO:0000256|ARBA:ARBA00039088};
GN ORFNames=F751_0364 {ECO:0000313|EMBL:KFM23006.1};
OS Auxenochlorella protothecoides (Green microalga) (Chlorella
OS protothecoides).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Auxenochlorella.
OX NCBI_TaxID=3075 {ECO:0000313|EMBL:KFM23006.1, ECO:0000313|Proteomes:UP000028924};
RN [1] {ECO:0000313|EMBL:KFM23006.1, ECO:0000313|Proteomes:UP000028924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0710 {ECO:0000313|EMBL:KFM23006.1,
RC ECO:0000313|Proteomes:UP000028924};
RX PubMed=25012212; DOI=10.1186/1471-2164-15-582;
RA Gao C., Wang Y., Shen Y., Yan D., He X., Dai J., Wu Q.;
RT "Oil accumulation mechanisms of the oleaginous microalga Chlorella
RT protothecoides revealed through its genome, transcriptomes, and
RT proteomes.";
RL BMC Genomics 15:582-582(2014).
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL662085; KFM23006.1; -; Genomic_DNA.
DR RefSeq; XP_011395873.1; XM_011397571.1.
DR AlphaFoldDB; A0A087SBA2; -.
DR STRING; 3075.A0A087SBA2; -.
DR GeneID; 23611755; -.
DR KEGG; apro:F751_0364; -.
DR eggNOG; KOG1158; Eukaryota.
DR OrthoDB; 9164at2759; -.
DR Proteomes; UP000028924; Unassembled WGS sequence.
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 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:UP000028924}.
FT DOMAIN 6..150
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 231..472
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 622 AA; 66523 MW; 6EB0EA32E4D1E836 CRC64;
MRQPPVTVLY GSQTGTAQEI AQNIGGRARE LGLVAKVAAL DEFGLDALTP ATVPVLVLVS
SSTGDGDPPD NAARFYGQIK KRGQQPDRLK GMTFTVLGLG DSNYTQFCRV PRALRSQVLA
LGAGEFHPGK DADEVDGLED VVEAWLDQML PALKRACLPT VAAEAASEGL KEPVPPEHAA
STKPVPLPEC RIEVEWLTDR SATQAVLDKE AAGATAEEVG HRDPEGLYSP EQPFHAPLIA
ARWLTTSAAG DRRVLHCELG VEGSGARTHP GDSLGVKPAN PPALVSALAA RLGLEASAVF
DVRPRPGVAT QHLLPHLHTP CSIGHALTES VDIAAPPRKS LLRLLAEHCA GEEARQTLLR
WTSRAGRDEY AKEVLEGRPS LLDLLTRFDS RPPLAPLLDA LPALVPRLYS IANAAVAQPG
KVAMALSIVR FTKACGTEHE GVATTWLERT AAPLLQGSWK GTEGPTPAVP RIPIYFRSGF
LQDRRHRLAA AAPGFEAGPS WLFFGCRHPD QDYLYKQELE EFEADGTLSR LSVAFSRQQA
RKVYVQHLVE RHAHELAALL AHPAASIFVC GDGASMATGV NEALARVLTG PGAFASGADW
KAGAAALAAM AREGRYVRDI WS
//
