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Database: UniProt
Entry: A0A2Y9N9I6_DELLE
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ID   A0A2Y9N9I6_DELLE        Unreviewed;       356 AA.
AC   A0A2Y9N9I6;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=NADH-cytochrome b5 reductase {ECO:0000256|RuleBase:RU361226};
DE            EC=1.6.2.2 {ECO:0000256|RuleBase:RU361226};
GN   Name=LOC111175847 {ECO:0000313|RefSeq:XP_022431460.1,
GN   ECO:0000313|RefSeq:XP_022431461.1, ECO:0000313|RefSeq:XP_022431463.1,
GN   ECO:0000313|RefSeq:XP_022431464.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022431464.1};
RN   [1] {ECO:0000313|RefSeq:XP_022431460.1, ECO:0000313|RefSeq:XP_022431461.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022431460.1,
RC   ECO:0000313|RefSeq:XP_022431461.1};
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
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|RuleBase:RU361226};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR601834-1, ECO:0000256|RuleBase:RU361226};
CC   -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC       reductase family. {ECO:0000256|ARBA:ARBA00006105,
CC       ECO:0000256|RuleBase:RU361226}.
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DR   RefSeq; XP_022431460.1; XM_022575752.2.
DR   RefSeq; XP_022431461.1; XM_022575753.2.
DR   RefSeq; XP_022431463.1; XM_022575755.2.
DR   RefSeq; XP_022431464.1; XM_022575756.2.
DR   STRING; 9749.A0A2Y9N9I6; -.
DR   Ensembl; ENSDLET00000028813; ENSDLEP00000026198; ENSDLEG00000018968.
DR   KEGG; dle:111175847; -.
DR   OrthoDB; 979728at2759; -.
DR   Proteomes; UP000248483; Unplaced.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IEA:UniProtKB-EC.
DR   CDD; cd06183; cyt_b5_reduct_like; 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; IPR001834; CBR-like.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR019180; Oxidoreductase-like_N.
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:SF184; NADH-CYTOCHROME B5 REDUCTASE-LIKE; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF09791; Oxidored-like; 1.
DR   PRINTS; PR00406; CYTB5RDTASE.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR601834-1};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR601834-
KW   1}; NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU361226};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU361226};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248483}.
FT   DOMAIN          116..218
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         167
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT   BINDING         169
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT   BINDING         184
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT   BINDING         186
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT   BINDING         193
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT   BINDING         194
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
SQ   SEQUENCE   356 AA;  39442 MW;  09CA31CFC790AB3D CRC64;
     MKSGEKEQPG VLRDQAGKGG GPGPTLGRAP SCPHLLPDQG PLTMDKGEED DDEEAWLQLR
     PVEPLPSQCC GSGCSPCVFD LYQRDLASWE AARASKDRSL LSGEETQSCP SKLSPETFLA
     FCISATDRLT KDTYLVRFAL PGNSRLGLRP GQHLILRGIV DGLEIQRAYT PISPANAKGY
     FEVLIKCYQT GLMSQYVESW KAGDTAFWRG PFGGFFYKPN QYGELLMLAA GTGLAPMVPI
     LQSITDNAED ETFITLVGCF KTFEGIYLKT FLREQARFWN VRTFFVLSQE NSLEQLPWSY
     RDKTHFGRLG QDLIEELVGS CRRKPFALVC GSAEFTKDVA GYLLSAGLAE DSYFLF
//
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