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Protein

Glutamyl-tRNA reductase 2

Gene

hemA2

Organism
Koribacter versatilis (strain Ellin345)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).UniRule annotation

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

Catalytic activityi

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.UniRule annotation

Pathwayi: protoporphyrin-IX biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu).UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamyl-tRNA reductase 1 (hemA1), Glutamyl-tRNA reductase 2 (hemA2)
  2. Glutamate-1-semialdehyde 2,1-aminomutase (hemL)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu), the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei50NucleophileUniRule annotation1
Sitei96Important for activityUniRule annotation1
Binding sitei106SubstrateUniRule annotation1
Binding sitei117SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi186 – 191NADPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processPorphyrin biosynthesis
LigandNADP

Enzyme and pathway databases

BioCyciCKOR204669:G1G6H-2647-MONOMER
UniPathwayiUPA00251; UER00316

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase 2UniRule annotation (EC:1.2.1.70UniRule annotation)
Short name:
GluTR 2UniRule annotation
Gene namesi
Name:hemA2UniRule annotation
Ordered Locus Names:Acid345_2564
OrganismiKoribacter versatilis (strain Ellin345)
Taxonomic identifieri204669 [NCBI]
Taxonomic lineageiBacteriaAcidobacteriaAcidobacterialesAcidobacteriaceaeCandidatus Koribacter
Proteomesi
  • UP000002432 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003349991 – 436Glutamyl-tRNA reductase 2Add BLAST436

Proteomic databases

PRIDEiQ1INI5

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi204669.Acid345_2564

Structurei

3D structure databases

ProteinModelPortaliQ1INI5
SMRiQ1INI5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni49 – 52Substrate bindingUniRule annotation4
Regioni111 – 113Substrate bindingUniRule annotation3

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

eggNOGiENOG4105C7E Bacteria
COG0373 LUCA
HOGENOMiHOG000109651
KOiK02492
OMAiFAFKCAA
OrthoDBiPOG091H05DA

Family and domain databases

Gene3Di3.30.460.30, 1 hit
HAMAPiMF_00087 Glu_tRNA_reductase, 1 hit
InterProiView protein in InterPro
IPR000343 4pyrrol_synth_GluRdtase
IPR015896 4pyrrol_synth_GluRdtase_dimer
IPR015895 4pyrrol_synth_GluRdtase_N
IPR018214 GluRdtase_CS
IPR036453 GluRdtase_dimer_dom_sf
IPR036343 GluRdtase_N_sf
IPR036291 NAD(P)-bd_dom_sf
IPR006151 Shikm_DH/Glu-tRNA_Rdtase
PfamiView protein in Pfam
PF00745 GlutR_dimer, 1 hit
PF05201 GlutR_N, 1 hit
PF01488 Shikimate_DH, 1 hit
PIRSFiPIRSF000445 4pyrrol_synth_GluRdtase, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
SSF69075 SSF69075, 1 hit
SSF69742 SSF69742, 1 hit
TIGRFAMsiTIGR01035 hemA, 1 hit
PROSITEiView protein in PROSITE
PS00747 GLUTR, 1 hit

Sequencei

Sequence statusi: Complete.

Q1INI5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNFFVIGVNH KTAPVEVRER FAIPESRLPE ATKLLASYPG IEEGMIVSTC
60 70 80 90 100
NRVEMVARSV NGNADMRGFL KQLYNIDPAQ YEQYLYEYRS TEAVRHMFRV
110 120 130 140 150
ASSLDSMVVG EPQILGQVKE AYATARAVGA VSSQLDALLT RAFAVAKRVR
160 170 180 190 200
TDTSIASSSV SIASVAVELA KKIFGSLQGR SVYIVGAGKM CELAARHFVA
210 220 230 240 250
HGVEKIYVAN RTYERGVAFA KKFNGEAVPI EHLYETVDKA DIVLSSTGAP
260 270 280 290 300
IAIFRKEHGE KFLSRRKNRP MFFLDIAVPR DVDAKMNELD GIFVYDIDDL
310 320 330 340 350
QQVVHSHISD RKDEAAHAEA IVNAEVEKFE ERLRTLDVVP TIVSLQEHLE
360 370 380 390 400
TVRQAEIDRL RGRLGELSPE QEMAVDALTK GIINKIMHTP ITTLKTAAKE
410 420 430
PESTTVIELV KRIFNLHEKA KDETVKTGPP QSGPGK
Length:436
Mass (Da):48,410
Last modified:June 13, 2006 - v1
Checksum:i407B8A871D22A84C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000360 Genomic DNA Translation: ABF41565.1
RefSeqiWP_011523366.1, NC_008009.1

Genome annotation databases

EnsemblBacteriaiABF41565; ABF41565; Acid345_2564
KEGGiaba:Acid345_2564

Similar proteinsi

Entry informationi

Entry nameiHEM12_KORVE
AccessioniPrimary (citable) accession number: Q1INI5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 13, 2006
Last modified: March 28, 2018
This is version 87 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health