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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Mycobacterium lepromatosis
Status
Unreviewed-Annotation score: -Protein inferred from homologyi

Functioni

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

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

Catalytic activityi

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.UniRule annotationSAAS 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 annotationSAAS 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 bindingi189 – 194NADPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductaseUniRule annotationSAAS annotation
Biological processPorphyrin biosynthesisUniRule annotationSAAS annotation
LigandNADPUniRule annotationSAAS annotation

Enzyme and pathway databases

UniPathwayi
UPA00251;UER00316

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductaseUniRule annotationSAAS annotation (EC:1.2.1.70UniRule annotationSAAS annotation)
Short name:
GluTRUniRule annotation
Gene namesi
Name:hemAUniRule annotationImported
ORF Names:MLPM_2422Imported
OrganismiMycobacterium lepromatosisImported
Taxonomic identifieri480418 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000053699 Componenti: Unassembled WGS sequence

Interactioni

Subunit structurei

Homodimer.UniRule annotationSAAS annotation

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 156GlutR_NInterPro annotationAdd BLAST150
Domaini172 – 313Shikimate_DHInterPro annotationAdd BLAST142
Domaini328 – 426GlutR_dimerInterPro annotationAdd BLAST99

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni49 – 52Substrate bindingUniRule annotation4
Regioni114 – 116Substrate 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 annotationSAAS annotation

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.

A0A0F4ESK7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSILLFGVSH RSAPVSVLEQ LSLDGSDQIK IVDRVLQSPL VTEAMVLSTC
60 70 80 90 100
NRVEVYAVVE AFHAGLSAIG QVLSEYSAMP IGDLTKYAYV RYSEAAVEHL
110 120 130 140 150
FTVASGLDSA VVGEQQVLGQ VRRAYAAAEA NRAVGQVLHE VAQRALSVGK
160 170 180 190 200
RVHSETAIDA AGISMVSVAL GIAERTLGGL AGRTAVVIGA GAMGALSSLH
210 220 230 240 250
LTQANIGRIN VLNRSLSRAR QLAGKVGEAG VPADVRTLDQ LAEVLADADL
260 270 280 290 300
VVSCTGAVSP VVSLADVHHA LAAMRRDETT RPLVICDLGM PRDVDPAVAK
310 320 330 340 350
LPGVWVVDVD RVQREPSAHA SAADVDAARR IVAAEVATYL TRQRMAEVTP
360 370 380 390 400
TVTALRQRAA DVIEAELLRL DHRLPGLEST QREEVAHTVR RVVDKLLHAP
410 420 430 440 450
TVRIKQLASA PGGDSYTEAL RELFELDQTA VDAVATAGEL PVMVSGFGDA
460
TSRYGTSAAQ DSSKHHAD
Length:468
Mass (Da):49,431
Last modified:June 24, 2015 - v1
Checksum:i72BA6482478F6673
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JRPY01000106 Genomic DNA Translation: KJX74600.1
RefSeqiWP_045843817.1, NZ_JRPY01000106.1

Genome annotation databases

EnsemblBacteriaiKJX74600; KJX74600; MLPM_2422
PATRICifig|480418.6.peg.5200

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JRPY01000106 Genomic DNA Translation: KJX74600.1
RefSeqiWP_045843817.1, NZ_JRPY01000106.1

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiKJX74600; KJX74600; MLPM_2422
PATRICifig|480418.6.peg.5200

Enzyme and pathway databases

UniPathwayi
UPA00251;UER00316

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
ProtoNetiSearch...

Entry informationi

Entry nameiA0A0F4ESK7_9MYCO
AccessioniPrimary (citable) accession number: A0A0F4ESK7
Entry historyiIntegrated into UniProtKB/TrEMBL: June 24, 2015
Last sequence update: June 24, 2015
Last modified: November 7, 2018
This is version 21 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

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

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