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Q30S94

- HEM1_SULDN

UniProt

Q30S94 - HEM1_SULDN

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Protein

Glutamyl-tRNA reductase

Gene
hemA, Suden_0859
Organism
Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira denitrificans (strain ATCC 33889 / DSM 1251))
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 sitei51 – 511Nucleophile By similarity
Sitei100 – 1001Important for activity By similarity
Binding sitei110 – 1101Substrate By similarity
Binding sitei121 – 1211Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi190 – 1956NADP By similarity

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

BioCyciSDEN326298:GH9P-900-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:Suden_0859
OrganismiSulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira denitrificans (strain ATCC 33889 / DSM 1251))
Taxonomic identifieri326298 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeSulfurimonas
ProteomesiUP000002714: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 432432Glutamyl-tRNA reductaseUniRule annotationPRO_1000071250Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi326298.Suden_0859.

Structurei

3D structure databases

ProteinModelPortaliQ30S94.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 534Substrate binding By similarity
Regioni115 – 1173Substrate 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.
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.
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.

Q30S94-1 [UniParc]FASTAAdd to Basket

« Hide

MHYLNISFSH KNSTLDVREK LSYKDDYATK GCLSKLNSGE SINESILIST    50
CNRMEVFCSC SDIASATKHI FEMLAARSGV SIDELEGRAD IFDDSSAIHH 100
LFSVASSLDS MVIGETQIAG QLKDAFRFSY DNGFCSQKLA RAMHHAFKCA 150
AKVRNATDIS SKPVSIASVA VSKLKSVLDN VEGKKALVIG VGEMSEITAK 200
HLLSSGADVY ITNRTKHKAE KLASECGAKV LDMQDLHKAV NEFEILFTAT 250
SSSEPIITDE IIKPCDFDRY WFDMAVPRDI NYHKGDRINL YVVDDLKNIV 300
DQNMSFREDG ARKAHGIIGR STVEFFEWLN TLNIEPMIKE IYEKAFEAAR 350
IESQRVIKKG FIPKEYEDQI HKMSQQVLKR FLHQMSSKMR SVSEESKADM 400
LTSAVQFLIE KDQRDIPDKY KCEHALNIIE GR 432
Length:432
Mass (Da):48,684
Last modified:December 6, 2005 - v1
Checksum:iDD46F339DB267FC2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000153 Genomic DNA. Translation: ABB44137.1.
RefSeqiWP_011372489.1. NC_007575.1.
YP_393372.1. NC_007575.1.

Genome annotation databases

EnsemblBacteriaiABB44137; ABB44137; Suden_0859.
GeneIDi3764130.
KEGGitdn:Suden_0859.
PATRICi23770296. VBISulDen68967_0889.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000153 Genomic DNA. Translation: ABB44137.1 .
RefSeqi WP_011372489.1. NC_007575.1.
YP_393372.1. NC_007575.1.

3D structure databases

ProteinModelPortali Q30S94.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 326298.Suden_0859.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABB44137 ; ABB44137 ; Suden_0859 .
GeneIDi 3764130.
KEGGi tdn:Suden_0859.
PATRICi 23770296. VBISulDen68967_0889.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.
KOi K02492.
OMAi HEVTGEY.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci SDEN326298:GH9P-900-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 33889 / DSM 1251.

Entry informationi

Entry nameiHEM1_SULDN
AccessioniPrimary (citable) accession number: Q30S94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: December 6, 2005
Last modified: September 3, 2014
This is version 73 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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