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Q2IJD4

- HEM11_ANADE

UniProt

Q2IJD4 - HEM11_ANADE

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Protein

Glutamyl-tRNA reductase 1

Gene

hemA1

Organism
Anaeromyxobacter dehalogenans (strain 2CP-C)
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 sitei49 – 491NucleophileUniRule annotation
Sitei93 – 931Important for activityUniRule annotation
Binding sitei103 – 1031SubstrateUniRule annotation
Binding sitei114 – 1141SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi183 – 1886NADPUniRule 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

BioCyciADEH290397:GI2Z-2023-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase 1UniRule annotation (EC:1.2.1.70UniRule annotation)
Short name:
GluTR 1UniRule annotation
Gene namesi
Name:hemA1UniRule annotation
Ordered Locus Names:Adeh_1994
OrganismiAnaeromyxobacter dehalogenans (strain 2CP-C)
Taxonomic identifieri290397 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeAnaeromyxobacteraceaeAnaeromyxobacter
ProteomesiUP000001935: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 422422Glutamyl-tRNA reductase 1PRO_0000335005Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi290397.Adeh_1994.

Structurei

3D structure databases

ProteinModelPortaliQ2IJD4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 514Substrate bindingUniRule annotation
Regioni108 – 1103Substrate 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.
HOGENOMiHOG000109650.
KOiK02492.
OMAiCINDENC.
OrthoDBiEOG6MWNBM.

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.

Q2IJD4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLVAVGLNQK GATVADREVL ALPSEELLDA LTAFQALDGV DEVAIVSTCY
60 70 80 90 100
RVEIFAAARC PAAAELSLRH ALEARAGRSL PLFELQGEEA FRHLVRVASS
110 120 130 140 150
LESAILGEPQ ILGQVKDAFH RAAEAGAAGK ELASVLSRAL AAAKRVRTET
160 170 180 190 200
AVGRAGVSWG NAAAALASKV LGPLAGRRVA VIGAGEMARL TAQHMRDERA
210 220 230 240 250
SVVVLNRTLA NAEALAAEVG GEARPLDALE QELLRADVVV SAAPAAPAAL
260 270 280 290 300
APAVMQRILH ARRKRIVMVD LAVPRAIPAE TGALPDVYLC DVDDLDRVMK
310 320 330 340 350
AAMAERAQAA QHAERIADEE VQKFARAEAE RRAAPLIQEM RSRASAIARE
360 370 380 390 400
EVERTLRRLG EDPELAKRLD AMAGSIVSKI LHAPSTRLRQ AVCDGGANDP
410 420
LVAAAVQIFD LSAAPAARGD AA
Length:422
Mass (Da):44,435
Last modified:March 7, 2006 - v1
Checksum:iB2F7050D3958C325
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000251 Genomic DNA. Translation: ABC81764.1.
RefSeqiWP_011421046.1. NC_007760.1.
YP_465201.1. NC_007760.1.

Genome annotation databases

EnsemblBacteriaiABC81764; ABC81764; Adeh_1994.
GeneIDi3887141.
KEGGiade:Adeh_1994.
PATRICi20920133. VBIAnaDeh31384_2046.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000251 Genomic DNA. Translation: ABC81764.1 .
RefSeqi WP_011421046.1. NC_007760.1.
YP_465201.1. NC_007760.1.

3D structure databases

ProteinModelPortali Q2IJD4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 290397.Adeh_1994.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABC81764 ; ABC81764 ; Adeh_1994 .
GeneIDi 3887141.
KEGGi ade:Adeh_1994.
PATRICi 20920133. VBIAnaDeh31384_2046.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109650.
KOi K02492.
OMAi CINDENC.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci ADEH290397:GI2Z-2023-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: 2CP-C.

Entry informationi

Entry nameiHEM11_ANADE
AccessioniPrimary (citable) accession number: Q2IJD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 7, 2006
Last modified: October 1, 2014
This is version 73 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