Skip Header

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

Glutamyl-tRNA reductase 2

Gene

hemA2

Organism
Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) (Clostridium phytofermentans)
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 2 (hemL2), Glutamate-1-semialdehyde 2,1-aminomutase 1 (hemL1)
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
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

BioCyciCPHY357809:G1GAJ-1845-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:Cphy_1784
OrganismiLachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) (Clostridium phytofermentans)
Taxonomic identifieri357809 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesLachnospiraceae
Proteomesi
  • UP000000370 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003350241 – 413Glutamyl-tRNA reductase 2Add BLAST413

Proteomic databases

PRIDEiA9KSC2

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi357809.Cphy_1784

Structurei

3D structure databases

ProteinModelPortaliA9KSC2
SMRiA9KSC2
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
HOGENOMiHOG000069583
KOiK02492
OMAiMANLVIK
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.

A9KSC2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNISMVGIDY NTASIEDREH FTLTSDKQLE IAKIIKETYH ASGCIILSTC
60 70 80 90 100
NRTEIWFSEL GTSEAECFHQ LVLGENAKET MRSICVCRQG DEAVTYLMEL
110 120 130 140 150
GCGIHSQIFG EDQILTQLKQ ALQQARDYQY VDSVLECLFR TAITAAKKVK
160 170 180 190 200
TSIQIAKGNT SLPQTIVEQL EKEQGDLLGK SCLVIGNGEM GRLMTEKLLE
210 220 230 240 250
KKCKVWMTLR QYKKSKAIIP EGSGVVLYDE RYEHIAVMDY IFSATKSHHF
260 270 280 290 300
TINKSMFENI RLKGKTYCLI DLAIPRDIEP SVEELSDVTV YNMDYFCQEV
310 320 330 340 350
NDREKELEET RELLSEYVNE FKQWYQFRNL VSTVDDISNI VSDITDAKLT
360 370 380 390 400
KVYKSIDLSR EQQELLQSNV QMAAKKAVSK IIFGLRDVLQ IDQCEEVLQA
410
LEQSAMNCTD SVK
Length:413
Mass (Da):47,150
Last modified:February 5, 2008 - v1
Checksum:i98276B1B10DCAAFA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000885 Genomic DNA Translation: ABX42154.1
RefSeqiWP_012199808.1, NC_010001.1

Genome annotation databases

EnsemblBacteriaiABX42154; ABX42154; Cphy_1784
KEGGicpy:Cphy_1784

Similar proteinsi

Entry informationi

Entry nameiHEM12_LACP7
AccessioniPrimary (citable) accession number: A9KSC2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: March 28, 2018
This is version 72 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

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health