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

Gene

hemA

Organism
Chloroflexus aurantiacus (strain ATCC 29364 / DSM 637 / Y-400-fl)
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 (hemA)
  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.

Pathwayi: chlorophyll biosynthesis

This protein is involved in the pathway chlorophyll biosynthesis, which is part of Porphyrin-containing compound metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway chlorophyll biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei55NucleophileUniRule annotation1
Sitei103Important for activityUniRule annotation1
Binding sitei113SubstrateUniRule annotation1
Binding sitei124SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi193 – 198NADPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processChlorophyll biosynthesis, Porphyrin biosynthesis
LigandNADP

Enzyme and pathway databases

BioCyciCSP480224:G1GUP-2871-MONOMER
UniPathwayiUPA00251; UER00316
UPA00668

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductaseUniRule annotation (EC:1.2.1.70UniRule annotation)
Short name:
GluTRUniRule annotation
Gene namesi
Name:hemAUniRule annotation
Ordered Locus Names:Chy400_2802
OrganismiChloroflexus aurantiacus (strain ATCC 29364 / DSM 637 / Y-400-fl)
Taxonomic identifieri480224 [NCBI]
Taxonomic lineageiBacteriaChloroflexiChloroflexiaChloroflexalesChloroflexineaeChloroflexaceaeChloroflexus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001905121 – 434Glutamyl-tRNA reductaseAdd BLAST434

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB9LKR5
SMRiB9LKR5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni54 – 57Substrate bindingUniRule annotation4
Regioni118 – 120Substrate 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

HOGENOMiHOG000109649
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
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

Sequencei

Sequence statusi: Complete.

B9LKR5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLFLAGLDH TTAPVEIREQ LAFSQTDLPS ALMQLTSSET GTPPLFAEAV
60 70 80 90 100
ILSTCNRVEL YGVTNPGTTA QHVVDFLAAF HRRPAASFVH TLYFYQGEAV
110 120 130 140 150
ARHLCATAAG LRSLVLGEAQ IQGQVRNAYE AAQRIGSVGS ILHRLFQIAL
160 170 180 190 200
VAGKRVRHET TIGKGAASVS QAGVELARRR LGDLRGREVL LIGGGEVSEL
210 220 230 240 250
AAQNLIANGA DRLTIVNRTS ARAAALAERY GAEMLDFGAL PQALARADIV
260 270 280 290 300
ISSTAAPVPI IYRHHVAEAI AHKQRARACG ECDPPTMLLI DLAVPRDIAA
310 320 330 340 350
DVAQIPGVHL FTVDDLREVV SHTIELRSAV LEIAQQIVEE QVQEFLSWMR
360 370 380 390 400
TQEALPVLTM LRQRAEEVRN EELARALRRL HDLSPEQRAV IEGLSRSIVN
410 420 430
KLLHPPTRCL REAAAHGQGK RYASILAELF NLEH
Length:434
Mass (Da):47,296
Last modified:March 24, 2009 - v1
Checksum:i1A101A099F18E489
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001364 Genomic DNA Translation: ACM54190.1
RefSeqiWP_015909256.1, NC_012032.1

Genome annotation databases

EnsemblBacteriaiACM54190; ACM54190; Chy400_2802
KEGGichl:Chy400_2802

Similar proteinsi

Entry informationi

Entry nameiHEM1_CHLSY
AccessioniPrimary (citable) accession number: B9LKR5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: March 28, 2018
This is version 60 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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