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A5ULU4

- HEM1_METS3

UniProt

A5ULU4 - HEM1_METS3

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Methanobrevibacter smithii (strain PS / ATCC 35061 / DSM 861)
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 sitei46 – 461NucleophileUniRule annotation
Sitei83 – 831Important for activityUniRule annotation
Binding sitei93 – 931SubstrateUniRule annotation
Binding sitei104 – 1041SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi173 – 1786NADPUniRule 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

BioCyciMSMI420247:GHWZ-992-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:Msm_0967
OrganismiMethanobrevibacter smithii (strain PS / ATCC 35061 / DSM 861)
Taxonomic identifieri420247 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanobrevibacter
ProteomesiUP000001992: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 399399Glutamyl-tRNA reductasePRO_1000004642Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi420247.Msm_0967.

Structurei

3D structure databases

ProteinModelPortaliA5ULU4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 484Substrate bindingUniRule annotation
Regioni98 – 1003Substrate 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.
OMAiKMLHGTM.

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.
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.

Sequencei

Sequence statusi: Complete.

A5ULU4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MILNLRVDHK IANIDAMENI AKEMDQLFLE LQEKYSIVEY VEISTCNRKE
60 70 80 90 100
YYIHNDNIDA SDSLLSHENK SIIIDYGDSV IKHLFRMTSG LESMIVGEDQ
110 120 130 140 150
ILGQVSDAKQ KAFKERHCGK ILDSIFTKAI HVGRVVRNKT NINKGSISIG
160 170 180 190 200
SAAVDLAEKH LGNLENKSVL VIGAGKMGKL VAKALAEKNL NAIFVANRTY
210 220 230 240 250
YVAVELANDL NGHAVLFNEL GKYVQTADLI ISATGAPHYI LNKERLEKTD
260 270 280 290 300
GDFKDLLMID IANPRDICED VCELGVKLFN IDDLREIADE NTKLRKKEFA
310 320 330 340 350
EAENIIDEEF SLLKESFKLI GVEDIIANLR VSMENIRERE TEKAIAKLSD
360 370 380 390
VDANAKIIDN LTNSIVNKIF FDISKKIKQA AHENDEELIR AIEFMFEEK
Length:399
Mass (Da):44,990
Last modified:July 10, 2007 - v1
Checksum:iF2BB1E52489E6504
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000678 Genomic DNA. Translation: ABQ87172.1.
RefSeqiYP_001273540.1. NC_009515.1.

Genome annotation databases

EnsemblBacteriaiABQ87172; ABQ87172; Msm_0967.
GeneIDi5217012.
KEGGimsi:Msm_0967.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000678 Genomic DNA. Translation: ABQ87172.1 .
RefSeqi YP_001273540.1. NC_009515.1.

3D structure databases

ProteinModelPortali A5ULU4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 420247.Msm_0967.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABQ87172 ; ABQ87172 ; Msm_0967 .
GeneIDi 5217012.
KEGGi msi:Msm_0967.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.
KOi K02492.
OMAi KMLHGTM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci MSMI420247:GHWZ-992-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.
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.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PS / ATCC 35061 / DSM 861.

Entry informationi

Entry nameiHEM1_METS3
AccessioniPrimary (citable) accession number: A5ULU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 10, 2007
Last modified: October 29, 2014
This is version 57 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