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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Rodentibacter heylii
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), Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA)
  2. Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), 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
Sitei104Important for activityUniRule annotation1
Binding sitei114SubstrateUniRule annotation1
Binding sitei125SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi199 – 204NADPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

UniPathwayiUPA00251; 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 annotation
ORF Names:BKG99_10065Imported
OrganismiRodentibacter heyliiImported
Taxonomic identifieri1906744 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeRodentibacter
Proteomesi
  • UP000188918 Componenti: Unassembled WGS sequence

Interactioni

Subunit structurei

Homodimer.UniRule annotationSAAS annotation

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 166GlutR_NInterPro annotationAdd BLAST161
Domaini182 – 320Shikimate_DHInterPro annotationAdd BLAST139
Domaini335 – 430GlutR_dimerInterPro annotationAdd BLAST96

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni49 – 52Substrate bindingUniRule annotation4
Regioni119 – 121Substrate bindingUniRule annotation3

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili352 – 383Sequence analysisAdd BLAST32

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

Keywords - Domaini

Coiled coilSequence analysis

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.

A0A1V3KDE1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLLVLGINH KTASVSVREK VAFSDEKRAL ALQQIQQQNL AEGAVILSTC
60 70 80 90 100
NRTEVYLHHR QISPQECDKW RQNVENWFAG IHQLALTDLL PSIYTHQNQQ
110 120 130 140 150
AANHLMRVAC GLDSLILGEP QILGQVKQAF QITEAYYQQS KVALSSEFSR
160 170 180 190 200
LFQKTFSTAK RVRTETNIGE SAVSVAYAAC SLARQIFESL HGVNILLVGA
210 220 230 240 250
GETIELVSRH LLRHGVKRLM IANRTVVKAE LLVEKLASNI PIDVFSLDQL
260 270 280 290 300
QEALEQADIV ISSTGSQNVL ISQDMVGLAQ KKRHYSPMLL VDIAVPRDID
310 320 330 340 350
ETVAKLDSVY HYTVDDLQDI IQRNLSQREQ ASQLAEGIIA QECEDFFEWL
360 370 380 390 400
KVRQFSNLIK HYREDAEQMR QELLEKALQH LRQGGSAETV LQELSYKLMN
410 420 430 440
KLIHAPTQTM QSMMKAGNAE GLHLFSNTLN LSHPLDEKNS
Length:440
Mass (Da):49,574
Last modified:June 7, 2017 - v1
Checksum:i44491A1BBDFA4D70
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
MLAD01000086 Genomic DNA Translation: OOF74472.1
RefSeqiWP_059368853.1, NZ_MLAD01000086.1

Similar proteinsi

Entry informationi

Entry nameiA0A1V3KDE1_9PAST
AccessioniPrimary (citable) accession number: A0A1V3KDE1
Entry historyiIntegrated into UniProtKB/TrEMBL: June 7, 2017
Last sequence update: June 7, 2017
Last modified: May 23, 2018
This is version 8 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

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