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Protein

NADH-cytochrome b5 reductase

Gene

CELE_T05H4.4

Organism
Caenorhabditis elegans
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5.UniRule annotation

Cofactori

FADUniRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotationSAAS annotation

Keywords - Ligandi

FADUniRule annotationSAAS annotation, Flavoprotein, NADUniRule annotationSAAS annotation

Enzyme and pathway databases

ReactomeiR-CEL-114608. Platelet degranulation.
R-CEL-1237044. Erythrocytes take up carbon dioxide and release oxygen.
R-CEL-196836. Vitamin C (ascorbate) metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
NADH-cytochrome b5 reductaseUniRule annotation (EC:1.6.2.2UniRule annotation)
Gene namesi
ORF Names:CELE_T05H4.4Imported, T05H4.4Imported
OrganismiCaenorhabditis elegansImported
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome V

Organism-specific databases

WormBaseiT05H4.4; CE13275; WBGene00020267.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei6 – 2520HelicalSequence analysisAdd
BLAST
Transmembranei173 – 19725HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Proteomic databases

EPDiO16522.
PaxDbiO16522.
PRIDEiO16522.

Interactioni

Protein-protein interaction databases

STRINGi6239.T05H4.4.

Structurei

3D structure databases

ProteinModelPortaliO16522.
SMRiO16522. Positions 37-303.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 154113FAD-binding FR-typeInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.UniRule annotation
Contains 1 FAD-binding FR-type domain.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helixSequence analysis

Phylogenomic databases

eggNOGiKOG0534. Eukaryota.
COG0543. LUCA.
GeneTreeiENSGT00390000008881.
HOGENOMiHOG000175005.
InParanoidiO16522.
KOiK00326.
OMAiGHINEEM.
OrthoDBiEOG7CZK69.
PhylomeDBiO16522.

Family and domain databases

InterProiIPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR001834. NADH-Cyt_B5_reductase.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00406. CYTB5RDTASE.
PR00371. FPNCR.
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O16522-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVENNTLAIT GGVVLISSVS LFLYLRQLRA EKKSKRTLED DSVKYLLPLI
60 70 80 90 100
EKFEISHNTR KFRFGLPSKD HILGLPIGHH VYLSANIGGK LIVRSYTPVS
110 120 130 140 150
CDLDLGYVDL MVKVYFKNTH ERFPDGGKMS QHLESLKIGD TVSFRGPHGS
160 170 180 190 200
IIYKGSGLFT VRMDKKAEPK NRFFKHLSMI AGGTGITPML QVIAAILRDP
210 220 230 240 250
IDATQIRLLF ANQTEDDILC RKELDELAEK HPTRFRVWYT VSKASKDWRY
260 270 280 290 300
STGHINEEMI KEHLFPSNEE SAVLLCGPPA MINCACIPNL DKLGHNSENY

LIF
Length:303
Mass (Da):34,264
Last modified:January 1, 1998 - v1
Checksum:i28F83123C650FD84
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX284605 Genomic DNA. Translation: CCD72031.1.
PIRiT31909.
RefSeqiNP_504639.1. NM_072238.1.
UniGeneiCel.2462.

Genome annotation databases

EnsemblMetazoaiT05H4.4; T05H4.4; WBGene00020267.
GeneIDi188150.
KEGGicel:CELE_T05H4.4.
UCSCiT05H4.4. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX284605 Genomic DNA. Translation: CCD72031.1.
PIRiT31909.
RefSeqiNP_504639.1. NM_072238.1.
UniGeneiCel.2462.

3D structure databases

ProteinModelPortaliO16522.
SMRiO16522. Positions 37-303.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6239.T05H4.4.

Proteomic databases

EPDiO16522.
PaxDbiO16522.
PRIDEiO16522.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiT05H4.4; T05H4.4; WBGene00020267.
GeneIDi188150.
KEGGicel:CELE_T05H4.4.
UCSCiT05H4.4. c. elegans.

Organism-specific databases

CTDi188150.
WormBaseiT05H4.4; CE13275; WBGene00020267.

Phylogenomic databases

eggNOGiKOG0534. Eukaryota.
COG0543. LUCA.
GeneTreeiENSGT00390000008881.
HOGENOMiHOG000175005.
InParanoidiO16522.
KOiK00326.
OMAiGHINEEM.
OrthoDBiEOG7CZK69.
PhylomeDBiO16522.

Enzyme and pathway databases

ReactomeiR-CEL-114608. Platelet degranulation.
R-CEL-1237044. Erythrocytes take up carbon dioxide and release oxygen.
R-CEL-196836. Vitamin C (ascorbate) metabolism.

Family and domain databases

InterProiIPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR001834. NADH-Cyt_B5_reductase.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00406. CYTB5RDTASE.
PR00371. FPNCR.
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    Caenorhabditis elegans Sequencing Consortium
    Sulson J.E., Waterston R.
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2Imported.

Entry informationi

Entry nameiO16522_CAEEL
AccessioniPrimary (citable) accession number: O16522
Entry historyi
Integrated into UniProtKB/TrEMBL: January 1, 1998
Last sequence update: January 1, 1998
Last modified: June 8, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.