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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Methanoregula boonei (strain 6A8)
Status
Reviewed-Annotation score: 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 sitei51 – 511NucleophileUniRule annotation
Sitei88 – 881Important for activityUniRule annotation
Binding sitei98 – 981SubstrateUniRule annotation
Binding sitei109 – 1091SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi178 – 1836NADPUniRule 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

BioCyciMBOO456442:GH2T-1259-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:Mboo_1238
OrganismiMethanoregula boonei (strain 6A8)
Taxonomic identifieri456442 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanoregulaceaeMethanoregula
ProteomesiUP000002408 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 424424Glutamyl-tRNA reductasePRO_0000335093Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi456442.Mboo_1238.

Structurei

3D structure databases

ProteinModelPortaliA7I7P5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 534Substrate bindingUniRule annotation
Regioni103 – 1053Substrate 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.
OMAiPIDVRER.

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.

A7I7P5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKHPSRFAV AGVSHHTADV LALEAFRFGD EPAFLAAAQK KFAGALLLQT
60 70 80 90 100
CNRVEVIVEG DAASLRDFLE SQERKGFFLL EGREALRHLF SLAAGIDSMI
110 120 130 140 150
VGEDQIIGQL KKSLADGEAA CTASPFLSLC INKAVHVGVG VRRTTKINRG
160 170 180 190 200
AVSVGSAAVL LAESELGTLE GRHILVVGSG EMGLLVAQAL AAKHLTAMYV
210 220 230 240 250
ANRTFGRAVI LAEKIGGVAV RMNELYHYIT LSDVVISCTS APHPVIHKTA
260 270 280 290 300
LKEAMRDRCW PVEGHPRPLI LVDIAQPRDV EEGAGAIDGV RLFTIDDLRQ
310 320 330 340 350
VNEQTMSTRR AEAERAAEYV DDELDLFIRQ LHRKSADDCI AALHTWAEAV
360 370 380 390 400
RVRERDRALA RLGNMDERTA GVIDDLSRVL TKKILTDATA SIRACAEEGD
410 420
RDAAEALVRA LTRGSAADSR EGTE
Length:424
Mass (Da):45,887
Last modified:September 10, 2007 - v1
Checksum:iD1275566FD0F4A09
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000780 Genomic DNA. Translation: ABS55756.1.
RefSeqiWP_012106787.1. NC_009712.1.
YP_001404399.1. NC_009712.1.

Genome annotation databases

EnsemblBacteriaiABS55756; ABS55756; Mboo_1238.
GeneIDi5409922.
KEGGimbn:Mboo_1238.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000780 Genomic DNA. Translation: ABS55756.1.
RefSeqiWP_012106787.1. NC_009712.1.
YP_001404399.1. NC_009712.1.

3D structure databases

ProteinModelPortaliA7I7P5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi456442.Mboo_1238.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABS55756; ABS55756; Mboo_1238.
GeneIDi5409922.
KEGGimbn:Mboo_1238.

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109651.
KOiK02492.
OMAiPIDVRER.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316.
BioCyciMBOO456442:GH2T-1259-MONOMER.

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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 6A8.

Entry informationi

Entry nameiHEM1_METB6
AccessioniPrimary (citable) accession number: A7I7P5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 19, 2008
Last sequence update: September 10, 2007
Last modified: March 31, 2015
This is version 61 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.