ID A0A2U4BJ95_TURTR Unreviewed; 349 AA.
AC A0A2U4BJ95;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=cytochrome-b5 reductase {ECO:0000256|ARBA:ARBA00012011};
DE EC=1.6.2.2 {ECO:0000256|ARBA:ARBA00012011};
GN Name=LOC101318394 {ECO:0000313|RefSeq:XP_019793297.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019793297.1};
RN [1] {ECO:0000313|RefSeq:XP_019793297.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019793297.1};
RG RefSeq;
RL Submitted (NOV-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|ARBA:ARBA00029341};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR601834-1};
CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC reductase family. {ECO:0000256|ARBA:ARBA00006105}.
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DR RefSeq; XP_019793297.1; XM_019937738.2.
DR AlphaFoldDB; A0A2U4BJ95; -.
DR GeneID; 101318394; -.
DR OrthoDB; 979728at2759; -.
DR Proteomes; UP000245320; Chromosome 1.
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; 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:SF171; 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 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|PIRSR:PIRSR601834-1};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR601834-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245320}.
FT DOMAIN 116..218
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..52
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 349 AA; 38850 MW; 0050FC23EE2E29D5 CRC64;
MKSREKEQPG VLRDQAGKGG GPGPALGRAP 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 VRTFFVLSQM KKLTLRGEGT
SWCRAARQGE ARIRTRDCLL PERQLSPTMV CCLPSTLWHP LLYGRGAWL
//
