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
Histophilus somni (strain 2336) (Haemophilus somnus)
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
Sitei104Important for activityUniRule annotation1
Binding sitei114SubstrateUniRule annotation1
Binding sitei125SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi201 – 206NADPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processPorphyrin biosynthesis
LigandNADP

Enzyme and pathway databases

BioCyciHSOM228400:G1GB8-1341-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:HSM_1279
OrganismiHistophilus somni (strain 2336) (Haemophilus somnus)
Taxonomic identifieri228400 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus
Proteomesi
  • UP000008543 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000931411 – 433Glutamyl-tRNA reductaseAdd BLAST433

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB0UU02
SMRiB0UU02
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

HOGENOMiHOG000109650
KOiK02492
OMAiFAFKCAA
OrthoDBiPOG091H05DA

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.

B0UU02-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTILVLGINH KTASVALREK VAFSDEKRLL ALKQIKQTQL AECAVILSTC
60 70 80 90 100
NRTEVYLHNK NVGPQNDEVW LDSCVQWFAD IHQVDLEELK SCLYSQQNLQ
110 120 130 140 150
ASRHLMRVAS GLDSLILGEP QILGQVKQAY QMSEEYYSLH SDIGMMSTEL
160 170 180 190 200
SRLFQKTFAT AKRVRTETHI GESAVSVAYA ACSLARQIFD SLRNLNILLV
210 220 230 240 250
GAGETIELVS RHLLRHGVNG LAIANRTLSR AEKLVEKLET TQKIDIFSLD
260 270 280 290 300
RLSEGLKRAD IVITSTGSPH VLISRNLIEQ AQQMRHYKPM LIVDIAVPRD
310 320 330 340 350
VEESAGEIES VYHYTVDDLH NIIQHNINQR EQASQQAEHI IQQESADFFE
360 370 380 390 400
WLKVHQFSNL IRNYRESAEI IRQDLLEKAL QALQNGENTE QVLQELSHKL
410 420 430
TKKLIHQPTQ AMQTMVKAGN TEGLQAFSHA VKS
Length:433
Mass (Da):49,006
Last modified:April 8, 2008 - v1
Checksum:i1CED8845C5397A13
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000947 Genomic DNA Translation: ACA31008.1
RefSeqiWP_012340438.1, NC_010519.1

Genome annotation databases

EnsemblBacteriaiACA31008; ACA31008; HSM_1279
GeneIDi31487581
KEGGihsm:HSM_1279

Similar proteinsi

Entry informationi

Entry nameiHEM1_HISS2
AccessioniPrimary (citable) accession number: B0UU02
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
Last modified: March 28, 2018
This is version 72 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

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

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