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A6UT22

- HEM1_META3

UniProt

A6UT22 - HEM1_META3

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Methanococcus aeolicus (strain Nankai-3 / ATCC BAA-1280)
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 sitei39 – 391NucleophileUniRule annotation
Sitei72 – 721Important for activityUniRule annotation
Binding sitei82 – 821SubstrateUniRule annotation
Binding sitei93 – 931SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi161 – 1666NADPUniRule 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

BioCyciMAEO419665:GHVZ-52-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:Maeo_0052
OrganismiMethanococcus aeolicus (strain Nankai-3 / ATCC BAA-1280)
Taxonomic identifieri419665 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus
ProteomesiUP000001106: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 383383Glutamyl-tRNA reductasePRO_1000004635Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi419665.Maeo_0052.

Structurei

3D structure databases

ProteinModelPortaliA6UT22.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni38 – 414Substrate bindingUniRule annotation
Regioni87 – 893Substrate 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.
OMAiEHMIEDE.

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.

A6UT22-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLLFRADYNN YAVSELQKLR FDEDEFYKKY DNCVLVQTCN RIEIYFDKNA
60 70 80 90 100
KIIDINEFAE FEMIKSNNAI KHLLRTASGL NSMIVGEDQI IGQIKNSHRK
110 120 130 140 150
AKELKKTTKY LDTIFLKAIH TGQKVRNNTK INKGCVSIGS AAVQLAEKTV
160 170 180 190 200
GLNNKNILVV GAGEIATLVA KALIEKNIRA IVVSNRTYER AELLAKKLNG
210 220 230 240 250
MAVHFDKLGE AINYNDIIIC ATGAPHAIID KDRLKNIKGY KVLIDIANPR
260 270 280 290 300
DVSDDVMELP NIKLYTIDDL KMVSEENLKK RKDEIPRVEK IIEEELSVLT
310 320 330 340 350
KQLRKLKFEN TIKNYDLYIE NLRKREMNKA LNMIENGKDP TVVLEKFSKV
360 370 380
FANKLISDFV NIVNDDTIGD IERVVNKLNK NKI
Length:383
Mass (Da):43,752
Last modified:August 21, 2007 - v1
Checksum:i24EA373469361A60
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000743 Genomic DNA. Translation: ABR55644.1.
RefSeqiYP_001324256.1. NC_009635.1.

Genome annotation databases

EnsemblBacteriaiABR55644; ABR55644; Maeo_0052.
GeneIDi5326829.
KEGGimae:Maeo_0052.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000743 Genomic DNA. Translation: ABR55644.1 .
RefSeqi YP_001324256.1. NC_009635.1.

3D structure databases

ProteinModelPortali A6UT22.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 419665.Maeo_0052.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABR55644 ; ABR55644 ; Maeo_0052 .
GeneIDi 5326829.
KEGGi mae:Maeo_0052.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci MAEO419665:GHVZ-52-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: Nankai-3 / ATCC BAA-1280.

Entry informationi

Entry nameiHEM1_META3
AccessioniPrimary (citable) accession number: A6UT22
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: October 29, 2014
This is version 59 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