Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q1ITN7

- HEM11_KORVE

UniProt

Q1ITN7 - HEM11_KORVE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glutamyl-tRNA reductase 1

Gene

hemA1

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).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 – 521NucleophileUniRule annotation
Sitei100 – 1001Important for activityUniRule annotation
Binding sitei110 – 1101SubstrateUniRule annotation
Binding sitei121 – 1211SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi190 – 1956NADPUniRule annotation

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 1UniRule annotation (EC:1.2.1.70UniRule annotation)
Short name:
GluTR 1UniRule annotation
Gene namesi
Name:hemA1UniRule annotation
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 1PRO_0000334998Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi204669.Acid345_0758.

Structurei

3D structure databases

ProteinModelPortaliQ1ITN7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni51 – 544Substrate bindingUniRule annotation
Regioni115 – 1173Substrate bindingUniRule annotation

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.UniRule annotation

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.UniRule annotation

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

« Hide

        10         20         30         40         50
MEPSLVVVGL NFKTSPVAVR ERFWMSELRR YEALHQLVRA EGIDELVVLA
60 70 80 90 100
TCNRTEFILW TSDAGEAADS VLRFLTHEYG LKMSDWSHFY RLMDDVALNH
110 120 130 140 150
IFRVASSLDS MVIGEPEIVG QFKNAWSQAQ AAGTTGRFLD AVMQKALTVS
160 170 180 190 200
KRVRNETAIG NAAVSIPYTT VELSKQVLGE LFDKAVVLMG AGKMSESAAK
210 220 230 240 250
YLMNHGASQI CVINRTLHKA QEFSEKVGGI AVALEDRAPY LDHADIIVSS
260 270 280 290 300
TSCPHYVIEK ADAERIQAAR GGKPIVMVDI AVPRDIDPAV REVPGVHLFD
310 320 330 340 350
MDDLEKVAKR NESERQVAAV AAEEILADEA KGFRRKLMAE RVVPTIVALR
360 370 380 390 400
NRLDEVCRQE LESLRQELGP FTEDQDQAMT ALTAHITQRI AGSLARELKE
410 420 430
LPERSEQDML TMAVQRLFHL EQPQKAAAGT N
Length:431
Mass (Da):47,868
Last modified:June 13, 2006 - v1
Checksum:i289915A299EE391E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: October 1, 2014
This is version 70 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.UniRule annotation

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