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Q0W5T5

- HEM1_UNCMA

UniProt

Q0W5T5 - HEM1_UNCMA

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Protein
Glutamyl-tRNA reductase
Gene
hemA, UNCMA_19350, RCIX911
Organism
Uncultured methanogenic archaeon RC-I
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 sitei49 – 491Nucleophile By similarity
Binding sitei99 – 991Substrate By similarity
Binding sitei110 – 1101Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi179 – 1846NADP 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

BioCyciUMET351160:GJT4-1985-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:UNCMA_19350
ORF Names:RCIX911
OrganismiUncultured methanogenic archaeon RC-I
Taxonomic identifieri351160 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanocellalesMethanocellaceaeMethanocella
ProteomesiUP000000663: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 427427Glutamyl-tRNA reductaseUniRule annotation
PRO_1000004720Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi351160.RCIX911.

Structurei

3D structure databases

ProteinModelPortaliQ0W5T5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 514Substrate binding By similarity
Regioni104 – 1063Substrate 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.
OMAiHEVTGEY.

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.

Q0W5T5-1 [UniParc]FASTAAdd to Basket

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MAQVCSISVN HRHAGIEGIE RARFRDPDVA MLRLLSLPGV SEAVVLQTCN    50
RVEIYAVAES VEDIVGFARA EGMPLEIAEV RAGDDCLKGL LRLACGLESM 100
IVGEDQILGQ LKTALLQARR LGTIGPVLST AIQKSIHVGA RARIETEINK 150
GSVSIGSAAV ELAESLLGDL RGRTILVVGA GEMGTLVANA MAEKSLRAIY 200
VANRTFEQAE KLASSLQGVA IRLERLCDYM GSADVVICAT GAPHLIITKK 250
MVEQCKGEKP LIFIDITNPR NIEETVGEVP GVTLHNIDSL RQINEASMRR 300
RQGEARKVEA IIEEELVLLQ RDIRRLHADR VIGDLYQRTD HIRATELRRA 350
VARLSTAGSL TEQQISILHD FSMALTNKIL AAPTRQLRRA AERCDEDCLR 400
TAEELFDLWV EESNGIPGNK TKASKTD 427
Length:427
Mass (Da):46,694
Last modified:September 5, 2006 - v1
Checksum:i4A31968C7217BAC7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM114193 Genomic DNA. Translation: CAJ36258.1.
RefSeqiYP_685584.1. NC_009464.1.

Genome annotation databases

EnsemblBacteriaiCAJ36258; CAJ36258; RCIX911.
GeneIDi5145812.
KEGGirci:RCIX911.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM114193 Genomic DNA. Translation: CAJ36258.1 .
RefSeqi YP_685584.1. NC_009464.1.

3D structure databases

ProteinModelPortali Q0W5T5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 351160.RCIX911.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAJ36258 ; CAJ36258 ; RCIX911 .
GeneIDi 5145812.
KEGGi rci:RCIX911.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci UMET351160:GJT4-1985-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. "Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere."
    Erkel C., Kube M., Reinhardt R., Liesack W.
    Science 313:370-372(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiHEM1_UNCMA
AccessioniPrimary (citable) accession number: Q0W5T5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 5, 2006
Last modified: May 14, 2014
This is version 66 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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