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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). In the absence of NADPH, exhibits substrate esterase activity, leading to the release of glutamate from tRNA.1 Publication

Catalytic activityi

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

Enzyme regulationi

Inhibited by heavy metal compounds, Zn2+, and heme. Also competitively inhibited by glutamycin.

pH dependencei

Optimum pH is 8.1.

Temperature dependencei

Optimum temperature is 90 degrees Celsius.

Pathwayi: protoporphyrin-IX biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu).
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamyl-tRNA reductase (hemA)
  2. Glutamate-1-semialdehyde 2,1-aminomutase (hemL)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu), the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei48Nucleophile1
Sitei84Important for activity1
Binding sitei94Substrate1
Binding sitei105Substrate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi174 – 179NADPCurated6

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.2.1.70. 3274.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:hemA
Ordered Locus Names:MK0200
OrganismiMethanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Taxonomic identifieri190192 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanopyriMethanopyralesMethanopyraceaeMethanopyrus
Proteomesi
  • UP000001826 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi48C → S: Complete loss of activity. 1 Publication1
Mutagenesisi84H → A: Complete loss of activity. 1 Publication1
Mutagenesisi84H → N: 30% of wild-type reductase activity. 15% of wild-type esterase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001141021 – 404Glutamyl-tRNA reductaseAdd BLAST404

Proteomic databases

PRIDEiQ9UXR8.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi190192.MK0200.

Structurei

Secondary structure

1404
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 10Combined sources7
Turni11 – 13Combined sources3
Helixi16 – 22Combined sources7
Helixi29 – 36Combined sources8
Beta strandi40 – 47Combined sources8
Beta strandi50 – 57Combined sources8
Helixi62 – 67Combined sources6
Beta strandi74 – 77Combined sources4
Helixi78 – 89Combined sources12
Turni90 – 93Combined sources4
Beta strandi94 – 96Combined sources3
Helixi100 – 116Combined sources17
Helixi121 – 140Combined sources20
Helixi150 – 162Combined sources13
Beta strandi169 – 174Combined sources6
Helixi177 – 189Combined sources13
Beta strandi192 – 197Combined sources6
Helixi201 – 211Combined sources11
Helixi218 – 220Combined sources3
Helixi221 – 226Combined sources6
Beta strandi229 – 233Combined sources5
Beta strandi236 – 239Combined sources4
Helixi244 – 253Combined sources10
Beta strandi260 – 264Combined sources5
Helixi275 – 277Combined sources3
Beta strandi281 – 285Combined sources5
Helixi286 – 301Combined sources16
Helixi304 – 350Combined sources47
Helixi365 – 382Combined sources18
Turni386 – 390Combined sources5
Helixi391 – 402Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GPJX-ray1.95A1-404[»]
ProteinModelPortaliQ9UXR8.
SMRiQ9UXR8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UXR8.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni47 – 50Substrate binding4
Regioni99 – 101Substrate binding3

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.Curated

Phylogenomic databases

eggNOGiarCOG01036. Archaea.
COG0373. LUCA.
HOGENOMiHOG000109651.
KOiK02492.
OMAiCNRYEIY.

Family and domain databases

Gene3Di1.10.1200.70. 1 hit.
3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase. 1 hit.
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.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UXR8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDLVCVGIT HKEAEVEELE KARFESDEAV RDIVESFGLS GCVLLQTCNR
60 70 80 90 100
VEVYASGARD RAEELGDLIH DDAWVKRGSE AVRHLFRVAC GLESMMVGEQ
110 120 130 140 150
EILRQVKKAY DRAARLGTLD EALKIVFRRA INLGKRAREE TRISEGAVSI
160 170 180 190 200
GSAAVELAER ELGSLHDKTV LVVGAGEMGK TVAKSLVDRG VRAVLVANRT
210 220 230 240 250
YERAVELARD LGGEAVRFDE LVDHLARSDV VVSATAAPHP VIHVDDVREA
260 270 280 290 300
LRKRDRRSPI LIIDIANPRD VEEGVENIED VEVRTIDDLR VIARENLERR
310 320 330 340 350
RKEIPKVEKL IEEELSTVEE ELEKLKERRL VADVAKSLHE IKDRELERAL
360 370 380 390 400
RRLKTGDPEN VLQDFAEAYT KRLINVLTSA IMELPDEYRR AACRALRRAS

ELNG
Length:404
Mass (Da):45,444
Last modified:May 1, 2000 - v1
Checksum:i8B6DBE436EA073B3
GO

Mass spectrometryi

Molecular mass is 45436±30 Da from positions 1 - 404. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ131561 Genomic DNA. Translation: CAB59204.1.
AE009439 Genomic DNA. Translation: AAM01417.1.
PIRiT45026.

Genome annotation databases

EnsemblBacteriaiAAM01417; AAM01417; MK0200.
KEGGimka:MK0200.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ131561 Genomic DNA. Translation: CAB59204.1.
AE009439 Genomic DNA. Translation: AAM01417.1.
PIRiT45026.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GPJX-ray1.95A1-404[»]
ProteinModelPortaliQ9UXR8.
SMRiQ9UXR8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi190192.MK0200.

Proteomic databases

PRIDEiQ9UXR8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM01417; AAM01417; MK0200.
KEGGimka:MK0200.

Phylogenomic databases

eggNOGiarCOG01036. Archaea.
COG0373. LUCA.
HOGENOMiHOG000109651.
KOiK02492.
OMAiCNRYEIY.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316.
BRENDAi1.2.1.70. 3274.

Miscellaneous databases

EvolutionaryTraceiQ9UXR8.

Family and domain databases

Gene3Di1.10.1200.70. 1 hit.
3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase. 1 hit.
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.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHEM1_METKA
AccessioniPrimary (citable) accession number: Q9UXR8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: May 1, 2000
Last modified: November 2, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.