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Database: UniProt
Entry: A0A131ZZM9_SARSC
LinkDB: A0A131ZZM9_SARSC
Original site: A0A131ZZM9_SARSC 
ID   A0A131ZZM9_SARSC        Unreviewed;       307 AA.
AC   A0A131ZZM9;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   28-JUN-2023, entry version 36.
DE   RecName: Full=NADH-cytochrome b5 reductase {ECO:0000256|RuleBase:RU361226};
DE            EC=1.6.2.2 {ECO:0000256|RuleBase:RU361226};
GN   ORFNames=QR98_0023980 {ECO:0000313|EMBL:KPM03959.1};
OS   Sarcoptes scabiei (Itch mite) (Acarus scabiei).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Sarcoptoidea;
OC   Sarcoptidae; Sarcoptinae; Sarcoptes.
OX   NCBI_TaxID=52283 {ECO:0000313|EMBL:KPM03959.1, ECO:0000313|Proteomes:UP000616769};
RN   [1] {ECO:0000313|EMBL:KPM03959.1, ECO:0000313|Proteomes:UP000616769}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Arlian Lab {ECO:0000313|EMBL:KPM03959.1};
RX   PubMed=26555130; DOI=10.1186/s13071-015-1198-2;
RA   Rider S.D.Jr., Morgan M.S., Arlian L.G.;
RT   "Draft genome of the scabies mite.";
RL   Parasit. Vectors 8:585-585(2015).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPM03959.1}.
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DR   EMBL; JXLN01006809; KPM03959.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A131ZZM9; -.
DR   VEuPathDB; VectorBase:SSCA005305; -.
DR   OMA; KGRFSYK; -.
DR   OrthoDB; 979728at2759; -.
DR   Proteomes; UP000616769; Unassembled WGS sequence.
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; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR19370; NADH-CYTOCHROME B5 REDUCTASE; 1.
DR   PANTHER; PTHR19370:SF185; NADH-CYTOCHROME B5 REDUCTASE; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00175; NAD_binding_1; 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}.
FT   BINDING         98
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT   BINDING         100
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT   BINDING         115
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT   BINDING         117
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT   BINDING         120
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT   BINDING         132
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT   BINDING         191
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
SQ   SEQUENCE   307 AA;  35383 MW;  630096FD0FFAB56C CRC64;
     MPFDTYPTFP LYMTGATILA TTIYFIYQFW KQNKEPKKPK LLENPKEKYS VALIEREEIS
     HDTRRFRFGL PSNDHVLGLP IGQHVYMSTT YQGKYISRSY TPVSSDDDRG YVDFVIKIYF
     ANVHPKFPDG GKLTQFLERM KIGDKINLAG PNGNLIYKGL GKFSIKEGYG SPFVNRSFKK
     IGMIAGGTGI TPMLQIIRHV FKDPKDKLSI WLLYANQTEK DILLRKELEE VQEKNSDRFK
     LWYTLDRPSE GWNYSTGFIN DEMISKHLPE PGKDTLILMC GPPPMIKHAC MPNLDKLGHL
     KQNCFAY
//
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