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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Clostridium botulinum (strain Alaska E43 / Type E3)
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 sitei46NucleophileUniRule annotation1
Sitei91Important for activityUniRule annotation1
Binding sitei101SubstrateUniRule annotation1
Binding sitei112SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi177 – 182NADPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processPorphyrin biosynthesis
LigandNADP

Enzyme and pathway databases

BioCyciCBOT508767:G1GC0-2578-MONOMER
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:CLH_2651
OrganismiClostridium botulinum (strain Alaska E43 / Type E3)
Taxonomic identifieri508767 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000931271 – 401Glutamyl-tRNA reductaseAdd BLAST401

Proteomic databases

PRIDEiB2UXC6

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

SMRiB2UXC6
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni45 – 48Substrate bindingUniRule annotation4
Regioni106 – 108Substrate 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

HOGENOMiHOG000090159
KOiK02492
OMAiFAFKCAA
OrthoDBiPOG091H05DA

Family and domain databases

Gene3Di3.30.460.301 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
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
SSF69742 SSF69742, 1 hit
TIGRFAMsiTIGR01035 hemA, 1 hit
PROSITEiView protein in PROSITE
PS00747 GLUTR, 1 hit

Sequencei

Sequence statusi: Complete.

B2UXC6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIAVLGIKRN TPIEIREKLT IKANKHDEYL DRLLKYLDGV IILATCNRTE
60 70 80 90 100
IYFNVSFINE ELLKKIFEIF NWNYSYRKYI FISEDKKACK HLFEVTCGFH
110 120 130 140 150
SKILGEDQIL GQVKTSYFKS LNAKALNLEL QRLFQYAITC GKKFKSQSRL
160 170 180 190 200
FEIPVSSASI VVNESINKDC KKFMVLGYGD VGRLTMKYLL AHNINEVYLA
210 220 230 240 250
VRNKKIKDEI VDERVNVIDF EEKNKYINDM DCVISCTSAP HIVIKKQDIN
260 270 280 290 300
NIGDNILIYD LAVPRDVDDE INDIDRAQVY NIDNISYIND GNKKMRFDKM
310 320 330 340 350
DSNKFILENY LNEYYEWKRL RSIAPFIEEL KVTSKEIYDK RITTFKNKCK
360 370 380 390 400
YRGDVDLANK MIKSTSDYYM NRAIEIMKEE TLKGSEEECL RIIKSIFIAK

K
Length:401
Mass (Da):47,076
Last modified:July 1, 2008 - v1
Checksum:i5F9C5007C65231D4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001078 Genomic DNA Translation: ACD52388.1
RefSeqiWP_012450542.1, NC_010723.1

Genome annotation databases

EnsemblBacteriaiACD52388; ACD52388; CLH_2651
KEGGicbt:CLH_2651

Similar proteinsi

Entry informationi

Entry nameiHEM1_CLOBA
AccessioniPrimary (citable) accession number: B2UXC6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 2008
Last modified: March 28, 2018
This is version 70 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program