ID S2JNI2_MUCC1 Unreviewed; 736 AA.
AC S2JNI2;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Methionine synthase reductase {ECO:0000256|ARBA:ARBA00040659};
DE EC=1.16.1.8 {ECO:0000256|ARBA:ARBA00039088};
GN ORFNames=HMPREF1544_03063 {ECO:0000313|EMBL:EPB90087.1};
OS Mucor circinelloides f. circinelloides (strain 1006PhL) (Mucormycosis
OS agent) (Calyptromyces circinelloides).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=1220926 {ECO:0000313|EMBL:EPB90087.1, ECO:0000313|Proteomes:UP000014254};
RN [1] {ECO:0000313|Proteomes:UP000014254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1006PhL {ECO:0000313|Proteomes:UP000014254};
RG The Broad Institute Genomics Platform;
RA Cuomo C., Earl A., Findley K., Lee S.C., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome sequence of Mucor circinelloides f. circinelloides 1006PhL.";
RL Submitted (MAY-2013) 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};
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DR EMBL; KE123925; EPB90087.1; -; Genomic_DNA.
DR AlphaFoldDB; S2JNI2; -.
DR STRING; 1220926.S2JNI2; -.
DR VEuPathDB; FungiDB:HMPREF1544_03063; -.
DR eggNOG; KOG1158; Eukaryota.
DR InParanoid; S2JNI2; -.
DR OMA; LFFGHQR; -.
DR OrthoDB; 9164at2759; -.
DR Proteomes; UP000014254; 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:UP000014254}.
FT DOMAIN 8..149
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 303..556
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 736 AA; 82439 MW; 36DEA0808B13ABF6 CRC64;
MVDLASEYLV LWASQTGNAE WIAKNIHTEA GNKGYKGECF VMDDFALAPL QKAGVIIIVS
SNTGDGDSPD NSLKFWRFLR RNKDKSYFAN TRFTVLGLGD SNYSNFNNSG KKLEKKFKDL
GGQVFYEKGL ADDAEGLENV VDPWIEKLWE VLPTVLRQEG NTSIESSIAH EKELEKEMSE
LAINPVDVPY SMKNRKKELP DLVEKYTNLE NTLVDNFTME ARREKLPGKV ADYTQLDNTL
VDGKKKIFKN GFPLTISLAG LEAGAKLTGL PRVSVPVAKV TKLDGQKAED FTGKVPDFVS
TPVPITYAPV TMVSCLTAPD AVKRTLEVEL DIGEDNHFEP GDAFGVLAPN DEELVEAILN
RLNVPEDEFH HLYKIEGENL PSHLQKANSA SLIELFRYAV DFTSHPRKAL FRMLADHTTD
PKEKLTLMYI CSKQGAAAFN AIRDESPTLL DILETFPSCH PPIDRLLDLL PAHMPRFYSI
SSSPLKRQGK IRFAFNVVEY ITAGKAERKG VATPWMDKIT KLIPSRSTPT NVEVAVTEDI
KVPMYIRQNA NAFVLPQETE RPLVLIGPGT GIAPFIGFLE HRQTQRNIRL SMGGIGHQPT
QQIWDQFGPI YVYYGFREKH KDFLFEKEIR EFEQDGTISL LRIAESRAAD APKVYVQDLI
KEDSAKLYDL IVNKDAAVYI CGDAKGMAKG VQDALAEMLV EHQKIDLLEA NKTLVNWIST
KKYLRDLVSG ICQVNA
//
