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Q022E5

- HEM1_SOLUE

UniProt

Q022E5 - HEM1_SOLUE

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Solibacter usitatus (strain Ellin6076)
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 sitei50 – 501NucleophileUniRule annotation
Sitei99 – 991Important for activityUniRule annotation
Binding sitei109 – 1091SubstrateUniRule annotation
Binding sitei120 – 1201SubstrateUniRule 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

BioCyciSUSI234267:GHSK-3207-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:Acid_3178
OrganismiSolibacter usitatus (strain Ellin6076)
Taxonomic identifieri234267 [NCBI]
Taxonomic lineageiBacteriaAcidobacteriaSolibacteresSolibacteralesSolibacteraceaeCandidatus Solibacter
ProteomesiUP000000671: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 421421Glutamyl-tRNA reductasePRO_0000335073Add
BLAST

Proteomic databases

PRIDEiQ022E5.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi234267.Acid_3178.

Structurei

3D structure databases

ProteinModelPortaliQ022E5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate bindingUniRule annotation
Regioni114 – 1163Substrate 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.
HOGENOMiHOG000109651.
KOiK02492.
OMAiLAHKLTN.
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.

Q022E5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLLITGVSH KTAPVEVREC LAFREETLPA ALADLKACEG VSEAVILSTC
60 70 80 90 100
NRVEISLTTE DAVDPREIVD NFLSRHKAVS SASIGPHLYR HEGRDAIHHL
110 120 130 140 150
FRVAASLDSM VVGEPQILGQ LKVAYAAAKD CGALCGWLDG LMSRSFSVAK
160 170 180 190 200
RVRSETGIGQ MAVSVSYAAV ELARKIFGSL TNRTVMIVGA GKMSELAARH
210 220 230 240 250
LRRSGASHVF VTNRTHERAV DMAKLFQGTP VEYARFTAML PEVDILIASS
260 270 280 290 300
GAPHYILHKD EMQRVISARR NKPMFLIDIA VPRNIEPAIN DLDNVFLYDI
310 320 330 340 350
DDLQEVVNSN LRERMKEADH AELLVTEEVD RMMARMKVAE VTPVIVSLQE
360 370 380 390 400
QLEQIRSGEM EKVRRRFGPF TAQQEEALEA LTRGIINKVA HGPISELRSQ
410 420
AGKPDGAPAI AAIRKAFHLQ D
Length:421
Mass (Da):46,431
Last modified:November 14, 2006 - v1
Checksum:iEB30E021342044C7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000473 Genomic DNA. Translation: ABJ84155.1.
RefSeqiYP_824440.1. NC_008536.1.

Genome annotation databases

EnsemblBacteriaiABJ84155; ABJ84155; Acid_3178.
GeneIDi4428635.
KEGGisus:Acid_3178.
PATRICi32008714. VBICanSol30224_3327.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000473 Genomic DNA. Translation: ABJ84155.1 .
RefSeqi YP_824440.1. NC_008536.1.

3D structure databases

ProteinModelPortali Q022E5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 234267.Acid_3178.

Proteomic databases

PRIDEi Q022E5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABJ84155 ; ABJ84155 ; Acid_3178 .
GeneIDi 4428635.
KEGGi sus:Acid_3178.
PATRICi 32008714. VBICanSol30224_3327.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci SUSI234267:GHSK-3207-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: Ellin6076.

Entry informationi

Entry nameiHEM1_SOLUE
AccessioniPrimary (citable) accession number: Q022E5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: November 14, 2006
Last modified: October 1, 2014
This is version 71 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