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A5ULU4

- HEM1_METS3

UniProt

A5ULU4 - HEM1_METS3

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Protein
Glutamyl-tRNA reductase
Gene
hemA, Msm_0967
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) By similarity.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 – 461Nucleophile By similarity
Sitei83 – 831Important for activity By similarity
Binding sitei93 – 931Substrate By similarity
Binding sitei104 – 1041Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi173 – 1786NADP By similarity

GO - Molecular functioni

  1. NADP binding Source: InterPro
  2. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP

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 reductase (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:hemA
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 reductaseUniRule annotation
PRO_1000004642Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi420247.Msm_0967.

Structurei

3D structure databases

ProteinModelPortaliA5ULU4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 484Substrate binding By similarity
Regioni98 – 1003Substrate binding By similarity

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 By similarity.UniRule annotation

Sequence similaritiesi

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

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MILNLRVDHK IANIDAMENI AKEMDQLFLE LQEKYSIVEY VEISTCNRKE    50
YYIHNDNIDA SDSLLSHENK SIIIDYGDSV IKHLFRMTSG LESMIVGEDQ 100
ILGQVSDAKQ KAFKERHCGK ILDSIFTKAI HVGRVVRNKT NINKGSISIG 150
SAAVDLAEKH LGNLENKSVL VIGAGKMGKL VAKALAEKNL NAIFVANRTY 200
YVAVELANDL NGHAVLFNEL GKYVQTADLI ISATGAPHYI LNKERLEKTD 250
GDFKDLLMID IANPRDICED VCELGVKLFN IDDLREIADE NTKLRKKEFA 300
EAENIIDEEF SLLKESFKLI GVEDIIANLR VSMENIRERE TEKAIAKLSD 350
VDANAKIIDN LTNSIVNKIF FDISKKIKQA AHENDEELIR AIEFMFEEK 399
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.
RefSeqiWP_011954208.1. NC_009515.1.
YP_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 WP_011954208.1. NC_009515.1.
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: September 3, 2014
This is version 55 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 By similarity.

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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