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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)
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 sitei49 – 491NucleophileUniRule annotation
Sitei90 – 901Important for activityUniRule annotation
Binding sitei100 – 1001SubstrateUniRule annotation
Binding sitei111 – 1111SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi180 – 1856NADPUniRule 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

BioCyciMBUR259564:GHBZ-1252-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:Mbur_1229
OrganismiMethanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)
Taxonomic identifieri259564 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanococcoides
ProteomesiUP000001979 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 422422Glutamyl-tRNA reductasePRO_1000004637Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi259564.Mbur_1229.

Structurei

3D structure databases

ProteinModelPortaliQ12WM5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 514Substrate bindingUniRule annotation
Regioni105 – 1073Substrate 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.

Q12WM5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEISSMVIT HAKATVEEME DSWHGDIDLV LSQLYSNELV YECAVLKTCN
60 70 80 90 100
RVEIYVVSSK GSSVLFHYAK EMGVSAKIVE FYDHDESLRH LLRLACGLES
110 120 130 140 150
MIIGEDQILG QIKDFFLMAK GAGTVGKVLS TAFSKAIQVG KRVRTETFIN
160 170 180 190 200
RGAVSIASAA VDLAEDILDG LNDKHILVIG TGEMGTLVTR ALSHRDMHVI
210 220 230 240 250
YLANRTYEKA RDLAEELGGE AVMFDQLEKY VRAADVVISA TSAPHYVLKG
260 270 280 290 300
DLVAKVMEGR ENELLLIDIA SPRDIDPAVE EIPHVILRNI DGLRVINEKN
310 320 330 340 350
LQMRMVEAKK AEIIIDDELD MVKAQYKRQK ADAIISNLYS QSHGLRHNEM
360 370 380 390 400
EHAINKLSAY HTIGEIERKV LEDLTHAITN KILAEPTKKL RNAAEYDDDK
410 420
FLDSVSRLFD IRPIKKNDGI TK
Length:422
Mass (Da):47,205
Last modified:August 21, 2006 - v1
Checksum:iA7621706C2763CE2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000300 Genomic DNA. Translation: ABE52151.1.
RefSeqiYP_565901.1. NC_007955.1.

Genome annotation databases

EnsemblBacteriaiABE52151; ABE52151; Mbur_1229.
GeneIDi3998553.
KEGGimbu:Mbur_1229.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000300 Genomic DNA. Translation: ABE52151.1.
RefSeqiYP_565901.1. NC_007955.1.

3D structure databases

ProteinModelPortaliQ12WM5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi259564.Mbur_1229.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABE52151; ABE52151; Mbur_1229.
GeneIDi3998553.
KEGGimbu:Mbur_1229.

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109651.
KOiK02492.
OMAiPIDVRER.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316.
BioCyciMBUR259564:GHBZ-1252-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: DSM 6242 / NBRC 107633 / OCM 468 / ACE-M.

Entry informationi

Entry nameiHEM1_METBU
AccessioniPrimary (citable) accession number: Q12WM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 14, 2008
Last sequence update: August 21, 2006
Last modified: March 31, 2015
This is version 72 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.