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Q0W5T5

- HEM1_UNCMA

UniProt

Q0W5T5 - HEM1_UNCMA

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Protein

Glutamyl-tRNA reductase

Gene

hemA

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).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
Binding sitei99 – 991SubstrateUniRule annotation
Binding sitei110 – 1101SubstrateUniRule annotation

Regions

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

BioCyciUMET351160:GJT4-1985-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: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 reductasePRO_1000004720Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi351160.RCIX911.

Structurei

3D structure databases

ProteinModelPortaliQ0W5T5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 514Substrate bindingUniRule annotation
Regioni104 – 1063Substrate 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.
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

« Hide

        10         20         30         40         50
MAQVCSISVN HRHAGIEGIE RARFRDPDVA MLRLLSLPGV SEAVVLQTCN
60 70 80 90 100
RVEIYAVAES VEDIVGFARA EGMPLEIAEV RAGDDCLKGL LRLACGLESM
110 120 130 140 150
IVGEDQILGQ LKTALLQARR LGTIGPVLST AIQKSIHVGA RARIETEINK
160 170 180 190 200
GSVSIGSAAV ELAESLLGDL RGRTILVVGA GEMGTLVANA MAEKSLRAIY
210 220 230 240 250
VANRTFEQAE KLASSLQGVA IRLERLCDYM GSADVVICAT GAPHLIITKK
260 270 280 290 300
MVEQCKGEKP LIFIDITNPR NIEETVGEVP GVTLHNIDSL RQINEASMRR
310 320 330 340 350
RQGEARKVEA IIEEELVLLQ RDIRRLHADR VIGDLYQRTD HIRATELRRA
360 370 380 390 400
VARLSTAGSL TEQQISILHD FSMALTNKIL AAPTRQLRRA AERCDEDCLR
410 420
TAEELFDLWV EESNGIPGNK TKASKTD
Length:427
Mass (Da):46,694
Last modified:September 5, 2006 - v1
Checksum:i4A31968C7217BAC7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: October 1, 2014
This is version 67 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