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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Actinobacillus pleuropneumoniae serovar 12 str. 1096
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
Sitei108Important for activityUniRule annotation1
Binding sitei118SubstrateUniRule annotation1
Binding sitei129SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi203 – 208NADPUniRule 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:appser12_4500Imported
OrganismiActinobacillus pleuropneumoniae serovar 12 str. 1096Imported
Taxonomic identifieri754261 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeActinobacillus
Proteomesi
  • UP000005464 Componenti: Unassembled WGS sequence

Interactioni

Subunit structurei

Homodimer.UniRule annotationSAAS annotation

Structurei

3D structure databases

ProteinModelPortaliE0FF68
SMRiE0FF68
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 170GlutR_NInterPro annotationAdd BLAST165
Domaini186 – 322Shikimate_DHInterPro annotationAdd BLAST137
Domaini336 – 430GlutR_dimerInterPro annotationAdd BLAST95

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni49 – 52Substrate bindingUniRule annotation4
Regioni123 – 125Substrate bindingUniRule annotation3

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili354 – 374Sequence analysisAdd BLAST21

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.

E0FF68-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTILALGINH KTASVNLRSK VAFDDQKRQL AFEQIQHRAL AESVVILSTC
60 70 80 90 100
NRTELYFHNA EITPREEHED NIAWREQCFE WFAEIHQLEH NELRECIYFK
110 120 130 140 150
QNMEAARHLM RVACGLDSLI LGEPQILGQV KQAYQYSENF YQSQNSHIST
160 170 180 190 200
KLSRLFQRTF STAKRVRSET EIGSSAVSVA YAACGLARQI FDNFGKLRFL
210 220 230 240 250
LVGAGETIEL VARYLIQHGA KNIMIANRTP QRAETLAERL NTPMQILSLS
260 270 280 290 300
ALQIGLNQAD IVISSTGSPD MLISKEMVEI AQKQRQFDPM LLIDIAVPRD
310 320 330 340 350
IDENAGELDA VYSYSVDDLQ HIIQRNMAQR EQAAEQAAQI VDEECKAFFE
360 370 380 390 400
WLKQQQSSDL IKRYRQDAEQ TRQELLAKAL VALTSGQDSE KVLNELSYKL
410 420 430
TNSLLHVPTQ ALQAMAKSGN SQGLQSFSKA LKLEEQ
Length:436
Mass (Da):49,451
Last modified:November 2, 2010 - v1
Checksum:i848A8392E81CA532
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
ADOL01000010 Genomic DNA Translation: EFN01237.1
RefSeqiWP_005596438.1, NZ_ADOL01000010.1

Genome annotation databases

EnsemblBacteriaiEFN01237; EFN01237; appser12_4500

Similar proteinsi

Entry informationi

Entry nameiE0FF68_ACTPL
AccessioniPrimary (citable) accession number: E0FF68
Entry historyiIntegrated into UniProtKB/TrEMBL: November 2, 2010
Last sequence update: November 2, 2010
Last modified: March 28, 2018
This is version 54 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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