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
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei50NucleophileUniRule annotation1
Sitei99Important for activityUniRule annotation1
Binding sitei109SubstrateUniRule annotation1
Binding sitei120SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi192 – 197NADPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processPorphyrin biosynthesis
LigandNADP

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316

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:SCO3319
ORF Names:SCE68.17c
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
Proteomesi
  • UP000001973 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001140761 – 581Glutamyl-tRNA reductaseAdd BLAST581

Proteomic databases

PRIDEiQ9WX15

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi100226.SCO3319

Structurei

3D structure databases

ProteinModelPortaliQ9WX15
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni49 – 52Substrate bindingUniRule annotation4
Regioni114 – 116Substrate bindingUniRule annotation3
Regioni292 – 416InsertAdd BLAST125

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
HOGENOMiHOG000109649
InParanoidiQ9WX15
KOiK02492
OMAiFAFKCAA
OrthoDBiPOG091H05DA
PhylomeDBiQ9WX15

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
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.

Q9WX15-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLLVVGLSH RSAPVSVLER ASLNADAQLK LLQDTVAAEP AAEAAVLATC
60 70 80 90 100
NRIELYADVD KFHAGVAELS TLLAQHSGVG LEELTPYLYV HYEDRAVHHL
110 120 130 140 150
FSVACGLDSM VVGEGQILGQ IKDSLARAQD LHTAGRLLND LFQQALRVGK
160 170 180 190 200
RAHSETGIDR AGQSLVTFGL EQLSAGADVE QWARGKKALV IGAGSMSSLA
210 220 230 240 250
AATLARAGVA EIVVANRTFE RAERLALLLE EQYGQRLSEG DDTDVLARAV
260 270 280 290 300
PMDAVPGELT RADVAVSCTG ATGLVLTADS VAATVEGRTG APAVEDTAVQ
310 320 330 340 350
ETAVREAGET PLPGAGSAAD ENCPLDLSSV SSVPSGFSVM GEAAVAGMDA
360 370 380 390 400
ATLEQHGAWA AGGTAVDRTR EAGRSGPEAD AELIGALAAT ATRVGRIPER
410 420 430 440 450
RRPEPVAEAP RPQPVLFLLD LAMPRDVDAA VHRLAGVRLV DIESLADASA
460 470 480 490 500
DAPMAADVDM VRRIVADEVA AFGAAQRAAH ITPTVVALRS MAADVVAGEI
510 520 530 540 550
ARLEGRLPGL DDKHRAEITQ TVKRVVDKLL HAPTVRVKQL AAEPGGAGYA
560 570 580
DALRTLFDLD QETVASVSRA ENSTEKNRGP A
Length:581
Mass (Da):60,562
Last modified:November 1, 1999 - v1
Checksum:iD4E256B105AFA037
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939116 Genomic DNA Translation: CAB45353.1
PIRiT36267
RefSeqiNP_627529.1, NC_003888.3
WP_011028907.1, NC_003888.3

Genome annotation databases

EnsemblBacteriaiCAB45353; CAB45353; CAB45353
GeneIDi1098753
KEGGisco:SCO3319
PATRICifig|100226.15.peg.3379

Similar proteinsi

Entry informationi

Entry nameiHEM1_STRCO
AccessioniPrimary (citable) accession number: Q9WX15
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: March 28, 2018
This is version 132 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health