ID V5B7R2_TRYCR Unreviewed; 484 AA.
AC V5B7R2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=cytochrome-b5 reductase {ECO:0000256|ARBA:ARBA00012011};
DE EC=1.6.2.2 {ECO:0000256|ARBA:ARBA00012011};
GN ORFNames=TCDM_08466 {ECO:0000313|EMBL:ESS63649.1};
OS Trypanosoma cruzi Dm28c.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=1416333 {ECO:0000313|EMBL:ESS63649.1, ECO:0000313|Proteomes:UP000017861};
RN [1] {ECO:0000313|EMBL:ESS63649.1, ECO:0000313|Proteomes:UP000017861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dm28c {ECO:0000313|EMBL:ESS63649.1,
RC ECO:0000313|Proteomes:UP000017861};
RX PubMed=24482508;
RA Grisard E.C., Teixeira S.M., de Almeida L.G., Stoco P.H., Gerber A.L.,
RA Talavera-Lopez C., Lima O.C., Andersson B., de Vasconcelos A.T.;
RT "Trypanosoma cruzi Clone Dm28c Draft Genome Sequence.";
RL Genome Announc. 2:e01114-13(2014).
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 -!- SIMILARITY: Belongs to the cytochrome b5 family.
CC {ECO:0000256|RuleBase:RU362121}.
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:ESS63649.1}.
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DR EMBL; AYLP01000118; ESS63649.1; -; Genomic_DNA.
DR AlphaFoldDB; V5B7R2; -.
DR EnsemblProtists; ESS63649; ESS63649; TCDM_08466.
DR VEuPathDB; TriTrypDB:TCDM_08466; -.
DR Proteomes; UP000017861; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU362121};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362121};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362121}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000017861}.
FT DOMAIN 50..126
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 129..205
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 223..324
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 484 AA; 52632 MW; 98C364B1C3ACDFF1 CRC64;
MGGIPSKKSV RNHGIDGVVK SSSNKAQGKK MEAPEAATAA TGKETAKTPS KTIGEAQVQN
MITQEGRDIV IIHGKVYDVT SFTASHPGGE AAIKSNVGKE AGETFESMHG SKAHERIEEF
LLGPLEVAPS VLTEFEVQRR ISEDKRVLLI IHGYVYDVTG FVASHPGGEA AIMSKLGEEV
GEVFERIHGK TTKELAKDFI VGRLSSTKVD VKDAAPKSPE VSKAVRETKV LESVDVAVDI
KNITFSCPEK LQIMPGGHIS VLVPDGSSNG FIKVSHYTPF VCEATSFTIT VKKYPNGMTS
SYLHSLKPGD TMKYEGPLRP NWVVEEDGAL RREQEDKRHV LFIAGGVGIT PIYTMVEHLL
KNQIASSTLV ASYQVPEVML LRKEFASLIE KYGKGAGKDV TEGEEVNVSP RKNFELHYVF
TRTKEAPIVS ETVNVHLGRF GAEVMKQLSP TVSCVICGPP SFADGIAKEL VKNNICNYQQ
VHVL
//
