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Q31IN7

- HEM1_THICR

UniProt

Q31IN7 - HEM1_THICR

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Protein

Glutamyl-tRNA reductase

Gene
hemA, Tcr_0390
Organism
Thiomicrospira crunogena (strain XCL-2)
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 sitei50 – 501Nucleophile By similarity
Sitei97 – 971Important for activity By similarity
Binding sitei107 – 1071Substrate By similarity
Binding sitei118 – 1181Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi187 – 1926NADP 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

BioCyciTCRU317025:GHE8-394-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:Tcr_0390
OrganismiThiomicrospira crunogena (strain XCL-2)
Taxonomic identifieri317025 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesPiscirickettsiaceaeThiomicrospira
ProteomesiUP000002713: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 434434Glutamyl-tRNA reductaseUniRule annotationPRO_1000004718Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi317025.Tcr_0390.

Structurei

3D structure databases

ProteinModelPortaliQ31IN7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni112 – 1143Substrate 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.
HOGENOMiHOG000109650.
KOiK02492.
OMAiLAHKLTN.
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.

Q31IN7-1 [UniParc]FASTAAdd to Basket

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MKLLVLGVNH ETAPVDIREK VSFSPAQVQN ALSELKSQGL ANESVILSTC    50
NRTEIYTTLK SQSPEKIRAW LHEYFELEED SINSFLYEYA DIEAIKHMMR 100
VSSGLNSLVL GEPQILGQIK EAFHLAHKSD SVHQTLHALF QYIFKTAKQV 150
RTDTAIGSSP VSVAFSAVAL SKQFFGKLEN QTALLLGAGE TVELVARHLK 200
ESHIGNLIIA NRTLSKAHQL TESLGGYAIS LHEIDDHLHE ADIVIASTAS 250
PTPILKTEMV ANALKKRRNK PMFMIDIAVP RDIEPAIGNF SDTYLYTVDD 300
LQEIIEENKR SRKDAALEAE EIVELQAENF MAQYQATQQI SPIIQRYRQQ 350
AYTLKEHALQ DALHHLENGG DPQELLTKLA NQLTNKILHT PTTNLHHAGL 400
NGQKEVIQAA EQILLTQQSD ASDSSENENT HATS 434
Length:434
Mass (Da):48,324
Last modified:December 6, 2005 - v1
Checksum:i2491058A27457AE6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000109 Genomic DNA. Translation: ABB40986.1.
RefSeqiWP_011369811.1. NC_007520.2.
YP_390660.1. NC_007520.2.

Genome annotation databases

EnsemblBacteriaiABB40986; ABB40986; Tcr_0390.
GeneIDi3760905.
KEGGitcx:Tcr_0390.
PATRICi23972668. VBIThiCru83387_0402.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000109 Genomic DNA. Translation: ABB40986.1 .
RefSeqi WP_011369811.1. NC_007520.2.
YP_390660.1. NC_007520.2.

3D structure databases

ProteinModelPortali Q31IN7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 317025.Tcr_0390.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABB40986 ; ABB40986 ; Tcr_0390 .
GeneIDi 3760905.
KEGGi tcx:Tcr_0390.
PATRICi 23972668. VBIThiCru83387_0402.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109650.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci TCRU317025:GHE8-394-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: XCL-2.

Entry informationi

Entry nameiHEM1_THICR
AccessioniPrimary (citable) accession number: Q31IN7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 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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