UniProt: A4IDQ0

Database: UniProt
Entry: A4IDQ0_LEIIN

LinkDB:  A4IDQ0_LEIIN 
Original site:  A4IDQ0_LEIIN

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (15)   
   InterPro (10)   
   Pfam (3)   
   PROSITE (2)   
Literature (2)   
   PubMed (2)   
All databases (24)   

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ID   A4IDQ0_LEIIN            Unreviewed;      1478 AA.
AC   A4IDQ0; A0A2K4Z8N7; A0A381MZS3;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=Methionine synthase reductase {ECO:0000256|ARBA:ARBA00040659};
DE            EC=1.16.1.8 {ECO:0000256|ARBA:ARBA00039088};
GN   ORFNames=LINJ_36_4950 {ECO:0000313|EMBL:CAM72983.1};
OS   Leishmania infantum.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5671 {ECO:0000313|EMBL:CAM72983.1, ECO:0000313|Proteomes:UP000008153};
RN   [1] {ECO:0000313|EMBL:CAM72983.1, ECO:0000313|Proteomes:UP000008153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPCM5 {ECO:0000313|EMBL:CAM72983.1,
RC   ECO:0000313|Proteomes:UP000008153};
RX   PubMed=17572675; DOI=10.1038/ng2053;
RA   Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA   Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA   Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA   Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA   Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA   Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA   Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA   Mottram J.C., Smith D.F., Berriman M.;
RT   "Comparative genomic analysis of three Leishmania species that cause
RT   diverse human disease.";
RL   Nat. Genet. 39:839-847(2007).
RN   [2] {ECO:0000313|EMBL:CAM72983.1, ECO:0000313|Proteomes:UP000008153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPCM5 {ECO:0000313|EMBL:CAM72983.1,
RC   ECO:0000313|Proteomes:UP000008153};
RX   PubMed=22038252; DOI=10.1101/gr.122945.111;
RA   Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA   Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA   Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA   Hertz-Fowler C., Mottram J.C.;
RT   "Chromosome and gene copy number variation allow major structural change
RT   between species and strains of Leishmania.";
RL   Genome Res. 21:2129-2142(2011).
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; FR796468; CAM72983.1; -; Genomic_DNA.
DR   RefSeq; XP_001469869.1; XM_001469832.1.
DR   AlphaFoldDB; A4IDQ0; -.
DR   SMR; A4IDQ0; -.
DR   STRING; 5671.A4IDQ0; -.
DR   GeneID; 5073975; -.
DR   KEGG; lif:LINJ_36_4950; -.
DR   VEuPathDB; TriTrypDB:LINF_360056700; -.
DR   eggNOG; KOG1158; Eukaryota.
DR   InParanoid; A4IDQ0; -.
DR   OMA; CYPRGEA; -.
DR   OrthoDB; 147634at2759; -.
DR   Proteomes; UP000008153; Chromosome 36.
DR   GO; GO:0030586; F:[methionine synthase] reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   CDD; cd06203; methionine_synthase_red; 1.
DR   Gene3D; 3.40.50.360; -; 3.
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; 3.
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   ECO:0000313|EMBL:CAM72983.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008153}.
SQ   SEQUENCE   1478 AA;  158088 MW;  91E3A13AE964AE9A CRC64;
     MSDETVFMDA GERLYVLYGS ETGNAESIAK RLHHDATNNH GFPDAACMTL NQAVSMKLFD
     AQLAEDAPAS LCVVIVCSTT GEGEPPQNAA RFRRWLRNAA GTLHKLRYCL LALGDTNYNS
     FCAPGIFMDN KLRDMGAVCC YPRGEADDNV GLHLVVNPWL EGLWSALKQS GTEGIAATGQ
     ETCATEDIRI DMSVAQEAAL LYSNSSPLCA ATALFLHERI TELGGKADLY PIQHFNPTTS
     LRRPPTVLFF VLGTEGDADA QCEQCACAAQ QLPPLGPLSA WIGNSDPCTP PPAEAVELHR
     WMSDPSIRFF NSLFVSRKPD GASRAAALDA DLKALATNCK LEYLCRCQLS GEVPSVAISA
     DDVFLWVEKV LHSLPGVTAD TVYIRRTMDD SFDTRVGAAF RAAHAPGLRS GSATESDYVA
     RGGSAPTLIG QRLYRVGLED DCGRGDAGHA SSENGGSHGA GASRKTHEVV DDLLTPIVFL
     YSGHSSFVKQ CAMNIFSGSG QHHLRCSISE LSNFQRMGFP RHATFVFIVS GVLTEPMSRV
     LKVLRTLQSQ KKDIEGVSFA ILGIGKTSES GRFNACALEL ETLLLKVKAN KIHCTGLADV
     DSSSLVPIVQ SWESSLWGAI VRPMKSTAYL DIASPGIQVQ RSVAPLATSG SSVGAALCLA
     GALVGESVIR DAGGNGGVGG GNDLVEHSKF GDFLSASASP SLLPLPGGVG PSRGADMQGS
     SLVTVPGSSL PGNSSTPTTV AAGATPGSDK TDASAAGAGL ADALSPWDTT PLHREKARHT
     PVVFLYASAG MSKAIAMHAM RSAEEKGFPT AVHPFAHFQF VDYHAHPNVM LFCEAGAEGQ
     TNGGRRFRKF LTNPSHHPGT LSSVRFAVLG LCATPADVVH PAFCWAKLLL RLQANRIFPV
     LIMPSISQLH SLGMPWINCV LSSLALLPSS VVVPSPPRGP NAPGAGELTI GPSRVGTAAA
     PRARDDDADN DAVEEAADAG EEVQRSVSAD MGSCGADVST EQDSCTEWSM ENRIAYRVDG
     VVQSWKLLTC PTVRHPVVQL DFSVSMGTQW APGQTIAVVP SNSTAQVEAL LRLFHLTRDE
     PFLPPAIAGP GVSVFPTSPL YEAVDFPVSC GTVLMRYVEL RVTGIHKPLF ELLARPCASE
     EAKAAVQTMY AELLADRTPR DLCEVLEAVG AAAHSLPPFR HIVENLSLLQ PRQYSICSSH
     RADATTLSIC FKVVEKGLCT RWMYEQCLSA AGLPLVSVAS AAPTHAEGCT APSAVRQPFL
     SNTAIVAKVR VVIPFEIRSA SVFRMPRDPL VPMILVGSGT GIAPFRAFLQ EREACLTERQ
     LPSGCTCPKG KLCGCSCEKA TRHGQAVCGT IDVFFGCRRR YEDYLFRDEL SHWKDSGVVH
     SLAVAFSRDT NDGRFYGGGC YVQDKIQECG VALMDLILQR NAYVFVCGDA DGMAKEVHRT
     LRQLIQQHLT LSDAAAATYL ERMSKDGRYL REVWSTGV
//

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