ID E9B0I6_LEIMU Unreviewed; 537 AA.
AC E9B0I6;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=cytochrome-b5 reductase {ECO:0000256|ARBA:ARBA00012011};
DE EC=1.6.2.2 {ECO:0000256|ARBA:ARBA00012011};
GN ORFNames=LMXM_29_0610 {ECO:0000313|EMBL:CBZ28741.1};
OS Leishmania mexicana (strain MHOM/GT/2001/U1103).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=929439 {ECO:0000313|EMBL:CBZ28741.1, ECO:0000313|Proteomes:UP000007259};
RN [1] {ECO:0000313|EMBL:CBZ28741.1, ECO:0000313|Proteomes:UP000007259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/GT/2001/U1103 {ECO:0000313|EMBL:CBZ28741.1,
RC ECO:0000313|Proteomes:UP000007259};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] +
CC H(+) + NAD(+); Xref=Rhea:RHEA:46680, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.2.2;
CC Evidence={ECO:0000256|ARBA:ARBA00029341};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; FR799582; CBZ28741.1; -; Genomic_DNA.
DR RefSeq; XP_003877208.1; XM_003877159.1.
DR AlphaFoldDB; E9B0I6; -.
DR GeneID; 13451387; -.
DR KEGG; lmi:LMXM_29_0610; -.
DR VEuPathDB; TriTrypDB:LmxM.29.0610; -.
DR OMA; KGAMQYS; -.
DR OrthoDB; 119434at2759; -.
DR PhylomeDB; E9B0I6; -.
DR Proteomes; UP000007259; Chromosome 29.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009703; F:nitrate reductase (NADH) activity; IEA:UniProtKB-EC.
DR CDD; cd00322; FNR_like; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 2.
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; IPR001834; CBR-like.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19370; NADH-CYTOCHROME B5 REDUCTASE; 1.
DR PANTHER; PTHR19370:SF171; NADH-CYTOCHROME B5 REDUCTASE-LIKE; 1.
DR Pfam; PF00173; Cyt-b5; 2.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00406; CYTB5RDTASE.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR PRINTS; PR00371; FPNCR.
DR SMART; SM01117; Cyt-b5; 2.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 2.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 2.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000313|EMBL:CBZ28741.1}.
FT DOMAIN 82..159
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 178..255
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 282..381
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 537 AA; 58199 MW; E4F2143833BDAC32 CRC64;
MGSKYARGII SSPAHEEERQ AHVDTEHHTE PPSSNAAAPE AEEMEATVTP TTPPTSTEQV
SMTVPGEEPS KRALPQKQHP RRKSFTMAEV QQLISVNPDR TLVIIRDRVY DVTTFLASHP
GGKSVLRRNN GKDVTDAFFS MHSATAVRKL PAFLIGELAP PESTSAAADE TPTAALVPAH
LRMADITKAL SEDPNRIILI LFSDAYDVTP MRDKHPGGLR VLTNSNGREC GDTFMRIHGP
LAKKMVRQFY LGPVEGAADV RSPLRPAVAV EAKSAVIPPA GTEVQSTRIL EMVPVNSTAT
IHYFTFSCPN PLDMIPGGHI RLYSNLYKEE SRFYTPFKTG VTSFTICMKH YPNGRTSGYF
FGLKEGCEVF FDGPLPPSWQ LNTDAAVQGA VPEERHVVLI AGGTGIVPLY SISSNALETQ
LSSVTLVCSV RTSEDLILAE ELRRLANRYS KALPSQKHTL RIVLLFSRAS PQDVSVESTS
FASHVLCGGR LTAESFKGIE IPPAQAVVVC GPPTFNDAVA GAVLESGICT AAQIHHL
//
