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Database: UniProt
Entry: A0A2P6TBL3_CHLSO
LinkDB: A0A2P6TBL3_CHLSO
Original site: A0A2P6TBL3_CHLSO 
ID   A0A2P6TBL3_CHLSO        Unreviewed;       285 AA.
AC   A0A2P6TBL3;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=NADH-cytochrome b5 reductase {ECO:0000256|RuleBase:RU361226};
DE            EC=1.6.2.2 {ECO:0000256|RuleBase:RU361226};
GN   ORFNames=C2E21_9416 {ECO:0000313|EMBL:PRW05938.1};
OS   Chlorella sorokiniana (Freshwater green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX   NCBI_TaxID=3076 {ECO:0000313|EMBL:PRW05938.1, ECO:0000313|Proteomes:UP000239899};
RN   [1] {ECO:0000313|EMBL:PRW05938.1, ECO:0000313|Proteomes:UP000239899}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX 1602 {ECO:0000313|Proteomes:UP000239899};
RX   PubMed=29178410; DOI=10.1111/tpj.13789;
RA   Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA   Barney B.M.;
RT   "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT   conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL   Plant J. 93:566-586(2018).
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|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:PRW05938.1}.
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DR   EMBL; LHPG02000027; PRW05938.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P6TBL3; -.
DR   STRING; 3076.A0A2P6TBL3; -.
DR   OrthoDB; 979728at2759; -.
DR   Proteomes; UP000239899; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF184; FAD-BINDING FR-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR19370; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU361226};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU361226};
KW   Reference proteome {ECO:0000313|Proteomes:UP000239899};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          50..154
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   BINDING         103
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT   BINDING         104
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT   BINDING         105
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         122
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT   BINDING         129
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         171
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
SQ   SEQUENCE   285 AA;  31618 MW;  3D1F8D4ADBA28A81 CRC64;
     MSQQALDELA LLVVHNLPQA LFVALVVFVV GLVLKDFING MARRPFLNPD KWQPLTLVDI
     KTLSHNTRRF RFALPHQEQE LGLPLGQHIS IKASDAEGRD VMRPYTPTTS VAQRGYVDFV
     IKLYPDGQMS QILAQADVGT TLLFKGPKGR FRYERGTKKA IGMIAGGSGI TPMFQVAQEI
     LNDPNDDTSL SLIYANVNED DILLRGELDE LAERHPNFSV YYVLNTPPRG WQGGKGFVTA
     DMIKKHLPAP GTDVLVLRCG PGPMNKAMEA HMDALGYTNG QQFQF
//
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