GenomeNet

Database: UniProt
Entry: A0A2Y9DJG3_TRIMA
LinkDB: A0A2Y9DJG3_TRIMA
Original site: A0A2Y9DJG3_TRIMA 
ID   A0A2Y9DJG3_TRIMA        Unreviewed;       305 AA.
AC   A0A2Y9DJG3;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=NADH-cytochrome b5 reductase {ECO:0000256|RuleBase:RU361226};
DE            EC=1.6.2.2 {ECO:0000256|RuleBase:RU361226};
GN   Name=LOC101360402 {ECO:0000313|RefSeq:XP_004375332.1};
OS   Trichechus manatus latirostris (Florida manatee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX   NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004375332.1};
RN   [1] {ECO:0000313|RefSeq:XP_004375332.1}
RP   IDENTIFICATION.
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|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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_004375332.1; XM_004375275.2.
DR   AlphaFoldDB; A0A2Y9DJG3; -.
DR   STRING; 127582.A0A2Y9DJG3; -.
DR   GeneID; 101360402; -.
DR   KEGG; tmu:101360402; -.
DR   InParanoid; A0A2Y9DJG3; -.
DR   OrthoDB; 979728at2759; -.
DR   Proteomes; UP000248480; Unplaced.
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:SF74; NADH-CYTOCHROME B5 REDUCTASE 1; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248480}.
FT   DOMAIN          44..156
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   BINDING         96
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT   BINDING         97
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT   BINDING         98
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT   BINDING         113
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         130
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT   BINDING         131
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         189
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
SQ   SEQUENCE   305 AA;  34052 MW;  FA50A1101DB97914 CRC64;
     MGIQPSPVLL ASLGVGLLTL LGLALGSYLV RRSRRPQVTL LDPNEKYLLR LLDKTTVSHN
     TKRFRFALPT AHHILGLPVG THVYLSARID GSLVIRPYTP VTSDEDRGYV DLVIKVYLKG
     VHPKFPEGGK MSQYLDSLKI GDMVEFRGPS GLLTYTGKGN FNIQPNKKSP PELRVANKLG
     MIAGGTGITP MLQLIQAILK DPEDPTQCFL LFANQTEKDI ILRDDLEELQ ARYPNRFKLW
     FTLDQPPEDW AFSKGFVTAN MIQDHLPAPG DDVLMLLCGP PPMVQLACHP NLDKLGYSQK
     MRFTY
//
DBGET integrated database retrieval system