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A4YD89

- HEM1_METS5

UniProt

A4YD89 - HEM1_METS5

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Protein
Glutamyl-tRNA reductase
Gene
hemA, Msed_0214
Organism
Metallosphaera sedula (strain ATCC 51363 / DSM 5348)
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 sitei53 – 531Nucleophile By similarity
Sitei98 – 981Important for activity By similarity
Binding sitei108 – 1081Substrate By similarity
Binding sitei119 – 1191Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi188 – 1936NADP 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

BioCyciMSED399549:GH1O-227-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:Msed_0214
OrganismiMetallosphaera sedula (strain ATCC 51363 / DSM 5348)
Taxonomic identifieri399549 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeMetallosphaera
ProteomesiUP000000242: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 424424Glutamyl-tRNA reductaseUniRule annotation
PRO_1000075413Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi399549.Msed_0214.

Structurei

3D structure databases

ProteinModelPortaliA4YD89.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni52 – 554Substrate binding By similarity
Regioni113 – 1153Substrate 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.
HOGENOMiHOG000107850.
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.
IPR018214. GluRdtase_CS.
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.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A4YD89-1 [UniParc]FASTAAdd to Basket

« Hide

MNPVNDIIDS YSAIVYTHKT VGVDKLASHY LGWNEIKELS KYYDGEMAVL    50
QTCNRIEIYL FSRNESSVNE ILHYLNEVHN KVISTDATIL RGEEAIKHLF 100
EVASGIDSLS VGEYEILKQI KDAMRDSIKL GIGSRYIRAL LERSLKVGRR 150
VRLETGISRG KVGVYSLAVE FAKSRFGDIL GKKIAILGAG EIGGKLALIL 200
HNEGATDVTI FNRTFERGRN LAIKYGYSYF PLDFSRLHNY DIIFSAIFYP 250
EKVKAPEGTV VIDLGSPPVF EGSNVYTLKD LEELSKATLE ERQREIERAE 300
SIIREGLEEF RKDCLNLVYD NFVSSFMSRV EETRKEEVER ALKVLGDDGE 350
ETREVLEAMT RSMIKKIFSP MFQNLRRAVE NNEINYINLA TSLLTHGGIS 400
QDKTKEIKTE QEYKGRSSGD ETDS 424
Length:424
Mass (Da):48,090
Last modified:May 29, 2007 - v1
Checksum:i3E18D902434B5E92
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000682 Genomic DNA. Translation: ABP94391.1.
RefSeqiWP_011921359.1. NC_009440.1.
YP_001190315.1. NC_009440.1.

Genome annotation databases

EnsemblBacteriaiABP94391; ABP94391; Msed_0214.
GeneIDi5104080.
KEGGimse:Msed_0214.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000682 Genomic DNA. Translation: ABP94391.1 .
RefSeqi WP_011921359.1. NC_009440.1.
YP_001190315.1. NC_009440.1.

3D structure databases

ProteinModelPortali A4YD89.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 399549.Msed_0214.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABP94391 ; ABP94391 ; Msed_0214 .
GeneIDi 5104080.
KEGGi mse:Msed_0214.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000107850.
KOi K02492.
OMAi EHMIEDE.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci MSED399549:GH1O-227-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.
IPR018214. GluRdtase_CS.
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.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism."
    Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.
    Appl. Environ. Microbiol. 74:682-692(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51363 / DSM 5348.

Entry informationi

Entry nameiHEM1_METS5
AccessioniPrimary (citable) accession number: A4YD89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 29, 2007
Last modified: September 3, 2014
This is version 60 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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