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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Chloroflexus aggregans (strain MD-66 / DSM 9485)
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

BioCyciCAGG326427:G1GUI-1291-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:Cagg_1288
OrganismiChloroflexus aggregans (strain MD-66 / DSM 9485)
Taxonomic identifieri326427 [NCBI]
Taxonomic lineageiBacteriaChloroflexiChloroflexiaChloroflexalesChloroflexineaeChloroflexaceaeChloroflexus
Proteomesi
  • UP000002508 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001905111 – 453Glutamyl-tRNA reductaseAdd BLAST453

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi326427.Cagg_1288

Structurei

3D structure databases

ProteinModelPortaliB8G817
SMRiB8G817
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

eggNOGiENOG4105C7E Bacteria
COG0373 LUCA
HOGENOMiHOG000109650
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.

B8G817-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLFLAGLDH TTAPVEIREQ LAFSQTDLPS ALLQLTQADN GSPPLFTEAV
60 70 80 90 100
ILSTCNRVEI YGVANPGTTA QHVVDFLANF HRRPAGSFVH TLYFYQGEAV
110 120 130 140 150
ARHLCATAAG LRSLVLGEAQ IQGQVRSAYE AAQRIGSVGS VLHRLFQIAL
160 170 180 190 200
VAGKRVRHET TIGKGAASVS QAGVELARRR LGDLRGREVL LIGGGEVSEL
210 220 230 240 250
AAQNLIANGA DRLTIVNRTS SRAAALAERY GAEMLDFGAL PEALARADIV
260 270 280 290 300
ISSTAAPVPI IYRHHIAEAL SHKQRMRACG DCDPPAMLLI DLAVPRDIAA
310 320 330 340 350
DVAELPGVYL FTVDDLREVV SHTIELRSAV IDIANQIVEE QVREFSDWLR
360 370 380 390 400
TQEALPVLTM LRQRAEEVRN EELTRALRRL HDLSPEQRAV IEGLSRSIVN
410 420 430 440 450
KLLHPPTRCL REAAAHGQGK RYATMLAELF NLEHALEHKA GAMGNTELTD

RMR
Length:453
Mass (Da):49,496
Last modified:March 3, 2009 - v1
Checksum:i4D3B325E808BA6CE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001337 Genomic DNA Translation: ACL24196.1
RefSeqiWP_012616560.1, NC_011831.1

Genome annotation databases

EnsemblBacteriaiACL24196; ACL24196; Cagg_1288
KEGGicag:Cagg_1288

Similar proteinsi

Entry informationi

Entry nameiHEM1_CHLAD
AccessioniPrimary (citable) accession number: B8G817
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: March 28, 2018
This is version 61 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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