ID A0A0V0ZGM2_9BILA Unreviewed; 745 AA.
AC A0A0V0ZGM2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Methionine synthase reductase {ECO:0000256|ARBA:ARBA00040659};
DE EC=1.16.1.8 {ECO:0000256|ARBA:ARBA00039088};
DE Flags: Fragment;
GN Name=tag-165 {ECO:0000313|EMBL:KRY11586.1};
GN ORFNames=T12_13461 {ECO:0000313|EMBL:KRY11586.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY11586.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY11586.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY11586.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY11586.1}.
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DR EMBL; JYDQ01000190; KRY11586.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0ZGM2; -.
DR STRING; 990121.A0A0V0ZGM2; -.
DR Proteomes; UP000054783; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR001611; Leu-rich_rpt.
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.
DR PROSITE; PS51450; LRR; 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}; Membrane {ECO:0000256|SAM:Phobius};
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:UP000054783};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 9..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..171
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 340..584
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY11586.1"
SQ SEQUENCE 745 AA; 85809 MW; 5E9DE98D7C1F5C10 CRC64;
LKRQYRYRYI YIYTCIYLCT KFMLNNFLIA YGSQTGQAKA IALRLSEKCQ AHNLTHRIHC
LSANEKEFCI EKERLVIFVV STTGDGEPPD SAHRFFTCLK RQVRQKQKSL SNLKFALLGL
GDSNYNTFCG APKALEKLLF QLHAKAFYPT GYCDEAVETA TVAEPWICGL LELLLSNNNL
DSIDKTLPLA KLSLEMENTE IASLGSTPER LNGIMTPRSN GRESQAIRCH METDPNYRYD
YYYDDDQRRR GDQSTVDPTI AHSPSMPSRR PRFYTFEECQ CRWAEPSVVG CEQLRNVIEL
KVPSMALIVP KLTSIVTHED YTQLNFPTTT PETEYAGQAS PRYMAKLLKR TVLTAPTAKK
TKVLLEFDLS GFDTPYKPGD AFSFICSNPQ NEVNWLLYRM NLSVLADKRC TLKLLPEAER
RGDKLPPYLP EVSSLRYLFT HCLDIRQSPS RILLRLFAEH CKTFGEKRRL MELCSSQGQQ
QYQRYIRRAG LSLMDVLHAF PSCLPPVDRL IELLPRLRPR PYSLACSPLV EEKRCNIVYS
LVSVTAEEGR FYARNGLATG YFETMQIGDQ IEMFLRQSSN FCLPSDILNT PIVMIGPGTG
VAPFISFLQH IKALSTEENR WCERWLFYGC QFESLDYIFR KQLEDFHDSF LLTHLVVSFS
KEEREDKAKY IQDSIRDNGF SLVRLLTEMN QSRVYVCGDV ENMAKEVFQA FVDILQSHGE
MSADDAKKFM SDLITNERYI LDYWL
//
