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Q2S2A5

- HEM1_SALRD

UniProt

Q2S2A5 - HEM1_SALRD

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Protein
Glutamyl-tRNA reductase
Gene
hemA, SRU_1555
Organism
Salinibacter ruber (strain DSM 13855 / M31)
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
Sitei94 – 941Important for activity By similarity
Binding sitei104 – 1041Substrate By similarity
Binding sitei115 – 1151Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi189 – 1946NADP 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

BioCyciSRUB309807:GJJD-1552-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:SRU_1555
OrganismiSalinibacter ruber (strain DSM 13855 / M31)
Taxonomic identifieri309807 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidetes Order II. Incertae sedisRhodothermaceaeSalinibacter
ProteomesiUP000008674: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 479479Glutamyl-tRNA reductaseUniRule annotation
PRO_0000335070Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi309807.SRU_1555.

Structurei

3D structure databases

ProteinModelPortaliQ2S2A5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 514Substrate binding By similarity
Regioni109 – 1113Substrate 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.
HOGENOMiHOG000106238.
KOiK02492.
OrthoDBiEOG6MWNBM.

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.

Q2S2A5-1 [UniParc]FASTAAdd to Basket

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MRFYAVGLNH ECTSLEQTET FALSAEEQEA LYANLSLSAD AEVVVLSTCN    50
RTEAYLYGTE ADLRQVKALI GQGGGTRWPE ETAFQERDEA AVRHLLQVTS 100
GLRSVVLGER QIFAQVKAAY ERAVDAGGIH SVMHRLFHTA FRAAKRVSSE 150
TGLGRGAASV STAAVEMARQ DLSEAGGEGL RNTEIVLVGA GKMGRLALEA 200
LADESLASLT VVNRSPDRAR EVASPFGGDT EPWADRHRAV ATADLALVAT 250
GASDPVLHAP ALPAPDEATL VVDVAMPRNV DPAVDERPGY RLYDLDDLEA 300
WTAEVRERRA DAVPEAESIC EELLEDFVTW VFHQQALQPA IQAIRSTFDT 350
IREQEVDRHA HRTGMDREEV DRLTESIMQK LLAVPIVRLK NVDPESIDFV 400
QGIELLHALF APSDESDAGR SLAEAPDADT PDLGEAPSRC PYMTHDPGGD 450
GTETEEVQKA LRLSAAHQAA SHSEEVRGG 479
Length:479
Mass (Da):51,933
Last modified:May 20, 2008 - v2
Checksum:iCCBDCF4F287BBB5D
GO

Sequence cautioni

The sequence ABC43868.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000159 Genomic DNA. Translation: ABC43868.1. Different initiation.
RefSeqiYP_445676.1. NC_007677.1.

Genome annotation databases

EnsemblBacteriaiABC43868; ABC43868; SRU_1555.
GeneIDi3851349.
KEGGisru:SRU_1555.
PATRICi23425545. VBISalRub86502_1609.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000159 Genomic DNA. Translation: ABC43868.1 . Different initiation.
RefSeqi YP_445676.1. NC_007677.1.

3D structure databases

ProteinModelPortali Q2S2A5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 309807.SRU_1555.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABC43868 ; ABC43868 ; SRU_1555 .
GeneIDi 3851349.
KEGGi sru:SRU_1555.
PATRICi 23425545. VBISalRub86502_1609.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000106238.
KOi K02492.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci SRUB309807:GJJD-1552-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: DSM 13855 / M31.

Entry informationi

Entry nameiHEM1_SALRD
AccessioniPrimary (citable) accession number: Q2S2A5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: May 14, 2014
This is version 73 of the entry and version 2 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, 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

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