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Q1ITN7

- HEM11_KORVE

UniProt

Q1ITN7 - HEM11_KORVE

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Protein

Glutamyl-tRNA reductase 1

Gene
hemA1, Acid345_0758
Organism
Koribacter versatilis (strain Ellin345)
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 sitei52 – 521Nucleophile 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

BioCyciKVER204669:GHL8-765-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase 1 (EC:1.2.1.70)
Short name:
GluTR 1
Gene namesi
Name:hemA1
Ordered Locus Names:Acid345_0758
OrganismiKoribacter versatilis (strain Ellin345)
Taxonomic identifieri204669 [NCBI]
Taxonomic lineageiBacteriaAcidobacteriaCandidatus Koribacter
ProteomesiUP000002432: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 431431Glutamyl-tRNA reductase 1UniRule annotationPRO_0000334998Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi204669.Acid345_0758.

Structurei

3D structure databases

ProteinModelPortaliQ1ITN7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni51 – 544Substrate 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.
OMAiCINDENC.
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.

Q1ITN7-1 [UniParc]FASTAAdd to Basket

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MEPSLVVVGL NFKTSPVAVR ERFWMSELRR YEALHQLVRA EGIDELVVLA    50
TCNRTEFILW TSDAGEAADS VLRFLTHEYG LKMSDWSHFY RLMDDVALNH 100
IFRVASSLDS MVIGEPEIVG QFKNAWSQAQ AAGTTGRFLD AVMQKALTVS 150
KRVRNETAIG NAAVSIPYTT VELSKQVLGE LFDKAVVLMG AGKMSESAAK 200
YLMNHGASQI CVINRTLHKA QEFSEKVGGI AVALEDRAPY LDHADIIVSS 250
TSCPHYVIEK ADAERIQAAR GGKPIVMVDI AVPRDIDPAV REVPGVHLFD 300
MDDLEKVAKR NESERQVAAV AAEEILADEA KGFRRKLMAE RVVPTIVALR 350
NRLDEVCRQE LESLRQELGP FTEDQDQAMT ALTAHITQRI AGSLARELKE 400
LPERSEQDML TMAVQRLFHL EQPQKAAAGT N 431
Length:431
Mass (Da):47,868
Last modified:June 13, 2006 - v1
Checksum:i289915A299EE391E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000360 Genomic DNA. Translation: ABF39763.1.
RefSeqiYP_589837.1. NC_008009.1.

Genome annotation databases

EnsemblBacteriaiABF39763; ABF39763; Acid345_0758.
GeneIDi4068634.
KEGGiaba:Acid345_0758.
PATRICi31978324. VBICanKor57425_0813.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000360 Genomic DNA. Translation: ABF39763.1 .
RefSeqi YP_589837.1. NC_008009.1.

3D structure databases

ProteinModelPortali Q1ITN7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 204669.Acid345_0758.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABF39763 ; ABF39763 ; Acid345_0758 .
GeneIDi 4068634.
KEGGi aba:Acid345_0758.
PATRICi 31978324. VBICanKor57425_0813.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci KVER204669:GHL8-765-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: Ellin345.

Entry informationi

Entry nameiHEM11_KORVE
AccessioniPrimary (citable) accession number: Q1ITN7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 13, 2006
Last modified: September 3, 2014
This is version 69 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, 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