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C3NF67

- HEM1_SULIN

UniProt

C3NF67 - HEM1_SULIN

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)
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
Sitei100 – 1001Important for activityUniRule annotation
Binding sitei110 – 1101SubstrateUniRule annotation
Binding sitei121 – 1211SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi190 – 1956NADPUniRule 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

BioCyciSISL419942:GHVO-865-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:YN1551_0841
OrganismiSulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2)
Taxonomic identifieri419942 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
ProteomesiUP000006818: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 426426Glutamyl-tRNA reductasePRO_1000202646Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi419942.YN1551_0841.

Structurei

3D structure databases

ProteinModelPortaliC3NF67.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni52 – 554Substrate bindingUniRule annotation
Regioni115 – 1173Substrate 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.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

C3NF67-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTSNEELLQN YCSILFTYKT IGISNLHLYY FRETEIKSLR QLINAEFAIL
60 70 80 90 100
QTCNRVEIYL YSNTNTISEI NKMIQYLNNV HNEPIGNQAR VICGKDSIKH
110 120 130 140 150
LFLVASGADS LSIGEYEILS QIRSTIDMFK KLGFSGKYLQ ILFERAIKVG
160 170 180 190 200
RKVREETSIS KGKVGIYSLA IDEAKRQFNN FYDRKIVIVG AGEMGQKIAN
210 220 230 240 250
MLYNEGVKNV TIMNRTVEKA KQLALKFGYN YEKLDLDKLG SFDIAFISIS
260 270 280 290 300
HENLRLENKW NTLIVDITVP PLFTGNNVIT LEELEKISKL NFKAREEELV
310 320 330 340 350
KINKLVEDGI DELIYDYKKE IYSEFMSKIM KRVETIRENE IVRAYKELEK
360 370 380 390 400
LGINNQQVKE ILDLMTRSII KKSFQPLFDN VRSLVFDGEN SINYINFLID
410 420
IFKDGNIPIF ETKKIKKKQI SKRSSS
Length:426
Mass (Da):49,336
Last modified:June 16, 2009 - v1
Checksum:i1C84F982D5E3DF96
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001404 Genomic DNA. Translation: ACP47963.1.
RefSeqiYP_002839885.1. NC_012623.1.

Genome annotation databases

EnsemblBacteriaiACP47963; ACP47963; YN1551_0841.
GeneIDi7809523.
KEGGisin:YN1551_0841.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001404 Genomic DNA. Translation: ACP47963.1 .
RefSeqi YP_002839885.1. NC_012623.1.

3D structure databases

ProteinModelPortali C3NF67.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 419942.YN1551_0841.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACP47963 ; ACP47963 ; YN1551_0841 .
GeneIDi 7809523.
KEGGi sin:YN1551_0841.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci SISL419942:GHVO-865-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.
TIGRFAMsi TIGR01035. hemA. 1 hit.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Y.N.15.51 / Yellowstone #2.

Entry informationi

Entry nameiHEM1_SULIN
AccessioniPrimary (citable) accession number: C3NF67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: June 16, 2009
Last modified: October 1, 2014
This is version 43 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

Documents

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

External Data

Dasty 3