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P43783

- GSHR_HAEIN

UniProt

P43783 - GSHR_HAEIN

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Protein
Glutathione reductase
Gene
gor, HI_0161
Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Maintains high levels of reduced glutathione in the cytosol By similarity.

Catalytic activityi

2 glutathione + NADP+ = glutathione disulfide + NADPH.

Cofactori

Binds 1 FAD per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei445 – 4451Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi34 – 429FAD By similarity

GO - Molecular functioni

  1. NADP binding Source: InterPro
  2. flavin adenine dinucleotide binding Source: InterPro
  3. glutathione-disulfide reductase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. glutathione metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione reductase (EC:1.8.1.7)
Short name:
GR
Short name:
GRase
Gene namesi
Name:gor
Ordered Locus Names:HI_0161
OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifieri71421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
ProteomesiUP000000579: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 456456Glutathione reductase
PRO_0000067976Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi42 ↔ 47Redox-active By similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer By similarity.

Protein-protein interaction databases

STRINGi71421.HI0161.

Structurei

3D structure databases

ProteinModelPortaliP43783.
SMRiP43783. Positions 2-456.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG1249.
KOiK00383.
OMAiHRQPCKM.
OrthoDBiEOG6QCD6D.
PhylomeDBiP43783.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006322. Glutathione_Rdtase_euk/bac.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSiPR00368. FADPNR.
SUPFAMiSSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01421. gluta_reduc_1. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P43783-1 [UniParc]FASTAAdd to Basket

« Hide

MTKHYDYIAI GGGSGGIASL NRAASYGKKC AIIEAKHLGG TCVNVGCVPK    50
KVMFYGAHIA EAINNYAPDY GFDVEVKKFD FSKLIESRQA YISRIHTSYN 100
NVLAKNNIDV INGFGKFVDA HTIEVTLADG TKEQVTADHI LIATGGRPYR 150
PNIKGQEYGI DSDGFFALTE LPKRAAVIGA GYIAVELSGV LNSLGVETHL 200
LVRRHAPMRN QDPLIVETLV EVLAQDGIQL HTNSTPSEIV KNADGSLTVR 250
CDGQSDVTVD CVIWAAGRVP TTDKIGLENA GVETNEHGYV KVDKYQNTNV 300
KGIYAVGDII ENGIELTPVA VAAGRRLSER LFNNKPTEYL DYSLVPTVVF 350
SHPPIGTVGL TEPQAIEQYG AENVKVYKSS FTAMYTAVTQ HRQPCKMKLV 400
CVGKDEKVVG LHGIGFGVDE MIQGFAVAIK MGATKADFDN TVAIHPTGSE 450
EFVTMR 456
Length:456
Mass (Da):49,329
Last modified:November 1, 1995 - v1
Checksum:i846988C215FE949A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U20229 Genomic DNA. Translation: AAA62137.1.
L42023 Genomic DNA. Translation: AAC21833.1.
PIRiA64052.
RefSeqiNP_438331.1. NC_000907.1.
WP_005694117.1. NC_000907.1.

Genome annotation databases

EnsemblBacteriaiAAC21833; AAC21833; HI_0161.
GeneIDi951071.
KEGGihin:HI0161.
PATRICi20188821. VBIHaeInf48452_0167.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U20229 Genomic DNA. Translation: AAA62137.1 .
L42023 Genomic DNA. Translation: AAC21833.1 .
PIRi A64052.
RefSeqi NP_438331.1. NC_000907.1.
WP_005694117.1. NC_000907.1.

3D structure databases

ProteinModelPortali P43783.
SMRi P43783. Positions 2-456.
ModBasei Search...

Protein-protein interaction databases

STRINGi 71421.HI0161.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC21833 ; AAC21833 ; HI_0161 .
GeneIDi 951071.
KEGGi hin:HI0161.
PATRICi 20188821. VBIHaeInf48452_0167.

Phylogenomic databases

eggNOGi COG1249.
KOi K00383.
OMAi HRQPCKM.
OrthoDBi EOG6QCD6D.
PhylomeDBi P43783.

Family and domain databases

Gene3Di 3.30.390.30. 1 hit.
InterProi IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006322. Glutathione_Rdtase_euk/bac.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view ]
Pfami PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view ]
PRINTSi PR00368. FADPNR.
SUPFAMi SSF55424. SSF55424. 1 hit.
TIGRFAMsi TIGR01421. gluta_reduc_1. 1 hit.
PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Barcak G.J., Heimer S.R.
    Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Entry informationi

Entry nameiGSHR_HAEIN
AccessioniPrimary (citable) accession number: P43783
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 3, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Haemophilus influenzae
    Haemophilus influenzae (strain Rd): entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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