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Q976H4

- HEM1_SULTO

UniProt

Q976H4 - HEM1_SULTO

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).UniRule annotation

Catalytic activityi

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei53 – 531NucleophileUniRule annotation
Sitei98 – 981Important for activityUniRule annotation
Binding sitei108 – 1081SubstrateUniRule annotation
Binding sitei119 – 1191SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi189 – 1946NADPUniRule annotation

GO - Molecular functioni

  1. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
  2. NADP binding Source: InterPro

GO - Biological processi

  1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciSTOK273063:GJC7-238-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductaseUniRule annotation (EC:1.2.1.70UniRule annotation)
Short name:
GluTRUniRule annotation
Gene namesi
Name:hemAUniRule annotation
Ordered Locus Names:STK_02120
OrganismiSulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Taxonomic identifieri273063 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
ProteomesiUP000001015: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 412412Glutamyl-tRNA reductasePRO_0000114111Add
BLAST

Proteomic databases

PRIDEiQ976H4.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi273063.ST0212.

Structurei

3D structure databases

ProteinModelPortaliQ976H4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni52 – 554Substrate bindingUniRule annotation
Regioni113 – 1153Substrate bindingUniRule annotation

Domaini

Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.UniRule annotation

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000107850.
KOiK02492.
OMAiEHMIEDE.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase.
InterProiIPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamiPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFiPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMiSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q976H4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSDEFIDINN YIAIVYTYKT VGISKLYEHY VKDQELLLLK GLIKGEISVL
60 70 80 90 100
QTCNRAETYL YTYNKEEFKD FLQKLDEIHG KQISKDAMIL KGEDAVKHLF
110 120 130 140 150
EVASGLDSLA IGEYEILRQL KESIEKSKKL GLSSEKLEFL FKNAIKVGRK
160 170 180 190 200
IRQQTEISKG KTGIYALAVE YAKHVSNNNI GNVKIAIVGA GEIGNKLALM
210 220 230 240 250
LKNEGAQNVT IFNRTYEKAL EVANKYGFKA EPLDFYKINN YDIVFVAIYY
260 270 280 290 300
DKKINLPNPK LVIDLSVPQI VLGNNVITLE NLRSISDKIM ETKILSLQKA
310 320 330 340 350
EELIHIEIEN FKNEIIKYNQ NRLISKFMKR IEDIREAEIN RAYAEILKHA
360 370 380 390 400
NDKEEIKNII DKMTNSMLKK IFSPLFETVR KNEDMANYIN NIFEILSNGN
410
ISNSKTEEAK EK
Length:412
Mass (Da):47,333
Last modified:December 1, 2001 - v1
Checksum:i37786BF228F36300
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000023 Genomic DNA. Translation: BAB65173.1.
RefSeqiNP_376064.1. NC_003106.2.
WP_010978155.1. NC_003106.2.

Genome annotation databases

EnsemblBacteriaiBAB65173; BAB65173; STK_02120.
GeneIDi1458103.
KEGGisto:ST0212.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000023 Genomic DNA. Translation: BAB65173.1 .
RefSeqi NP_376064.1. NC_003106.2.
WP_010978155.1. NC_003106.2.

3D structure databases

ProteinModelPortali Q976H4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 273063.ST0212.

Proteomic databases

PRIDEi Q976H4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB65173 ; BAB65173 ; STK_02120 .
GeneIDi 1458103.
KEGGi sto:ST0212.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000107850.
KOi K02492.
OMAi EHMIEDE.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci STOK273063:GJC7-238-MONOMER.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_00087. Glu_tRNA_reductase.
InterProi IPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view ]
Pfami PF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMi SSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 16993 / JCM 10545 / NBRC 100140 / 7.

Entry informationi

Entry nameiHEM1_SULTO
AccessioniPrimary (citable) accession number: Q976H4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: December 1, 2001
Last modified: October 1, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA.UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3